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Human Metabolome Database Version 2.5

 

Showing metabocard for Dextrin (HMDB06857)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-13 16:55:03
Update Date 2009-05-05 21:01:16
Accession Number HMDB06857
Secondary Accession Numbers Not Available
Common Name Dextrin
Description Dextrins are a group of low-molecular-weight carbohydrates produced by the hydrolysis of starch. Dextrins are mixtures of linear α-(1,4)-linked D-glucose polymers starting with an α-(1,6) bond. Because branched amylopectin and glycogen also contain α-(1,6) bonds, which α-amylase cannot hydrolyze in humans, the digest resulting from this action contains a mixture of dextrins. They have the same general formula as carbohydrates but are of shorter chain length. Industrial production is, in general, performed by acidic hydrolysis of potato starch. Dextrins are water-soluble, white to slightly yellow solids that are optically active. Under analysis, dextrins can be detected with iodine solution, giving a red coloration. The cyclical dextrins are known as cyclodextrins. They are formed by enzymatic degradation of starch by certain bacteria, for example, Bacillus macerans. Cyclodextrins have toroidal structures formed by 6-8 glucose residues. Dextrins find widespread use in industry, due to their non-toxicity and their low price. They are used as water-soluble glues, as thickening agents in food processing, and as binding agent in pharmaceuticals. In pyrotechnics, they are added to fire formulas, allowing them to solidify as pellets or "stars." Cyclodextrins find additional use in analytical chemistry as a matrix for the separation of hydrophobic substances, and as excipients in pharmaceutical formulations. Not all forms of dextrin are digestible, and indigestible dextrin is sometimes used in fiber supplements. For example, maltodextrin either can be moderately sweet or have hardly any flavor at all. Maltodextrin is a polysaccharide that is used as a food additive. It is produced from starch and is usually found as a creamy-white hygroscopic powder. Maltodextrin is easily digestible, being absorbed as rapidly as glucose. The CAS registry number of maltodextrin is 9050-36-6. Maltodextrin can be derived from any starch. In the US, this starch is usually rice, corn or potato; elsewhere, such as in Europe, it is commonly wheat. This is important for coeliacs, since the wheat-derived maltodextrin can contain traces of gluten. There have been recent reports of coeliac reaction to maltodextrin in the United States. This might be a consequence of the shift of corn to ethanol production and its replacement with wheat in the formulation. The fast food chain, Wendy's, footnotes maltodextrin in its list of gluten-free foods [1], which may be a sign of their receiving reports of this. Foods containing maltodextrin may contain traces of amino acids, including glutamic acid as a manufacturing by-product. The amino acid traces would be too small to have any dietary significance.(Wikipedia)
Synonyms
  1. Caloreen
  2. Dextrine
  3. Dextrins
  4. Fortodex
  5. Dextrid
  6. Dextrin
  7. Corn dextrin
  8. Dextrina Bianca
  9. British gum
  10. Crystal gum
Chemical IUPAC Name sodium (2-hydroxy-3-octadec-9-enoyloxypropyl) hydrogen phosphate
Chemical Formula C18H32O16
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Carbohydrates
Sub Class
  • Trisaccharides
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • acetal
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 504.437
Monoisotopic Molecular Weight 504.169037
Isomeric SMILES OC[C@H]1OC(O[C@@H]2[C@@H](CO)OC(O[C@@H]3[C@@H](CO)O[C@H](O)[C@H](O)[C@H]3O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(OC2C(CO)OC(OC3C(CO)OC(O)C(O)C3O)C(O)C2O)C(O)C(O)C1O
KEGG Compound ID C00721 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06857 Link Image
Metagene Link HMDB06857 Link Image
METLIN ID Not Available
PubChem Compound 62698 Link Image
PubChem Substance 3987 Link Image
ChEBI ID Not Available
CAS Registry Number 9004-53-9
InChI Identifier InChI=1/C18H32O16/c19-1-4-7(22)8(23)12(27)17(31-4)34-15-6(3-21)32-18(13(28)10(15)25)33-14-5(2-20)30-16(29)11(26)9(14)24/h4-29H,1-3H2/t4-,5-,6-,7-,8+,9-,10-,11-,12-,13-,14-,15-,16+,17?,18?/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 554.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.74 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Starch and Sucrose Metabolism SMP00058 Link Image map00500 Link Image
General References Not Available
Metabolic Enzymes
  1. Sucrase-isomaltase, intestinal
  2. Glycogen debranching enzyme
  3. Alpha-amylase 1
  4. Pancreatic alpha-amylase
  5. Alpha-amylase 2B
  6. Maltase-glucoamylase, intestinal
  7. Lysozyme-like protein 1
  8. cDNA FLJ45104 fis, clone BRAWH3032930, highly similar to Alpha-amylase 2B (EC 3.2.1.1)
Enzyme 1 [top]
Enzyme 1 ID 5523
Enzyme 1 Name Sucrase-isomaltase, intestinal
Enzyme 1 Synonyms
  1. Sucrase
  2. Isomaltase
Enzyme 1 Gene Name SI
Enzyme 1 Protein Sequence >Sucrase-isomaltase, intestinal
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDS
GKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMT
TTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEF
TGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISARLPSDYIYG
IGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSN
AMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRW
NYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQ
KYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNP
NCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMY
SKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAH
WLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSR
NHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHE
FYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDM
YLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDT
IQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMN
AHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGC
VWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRV
EVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRS
SGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPP
GYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGP
TPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDI
DYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVF
VKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVD
FYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEA
EQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGD
NYARWDNMDKSIIGMMEFSLFGISYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNI
ANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKP
TWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDT
INLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLY
LSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNE
DTTNMILRIDLTTHNVTLEEPIEINWS
Enzyme 1 Number of Residues 1827
Enzyme 1 Molecular Weight 209403.4
Enzyme 1 Theoretical pI 5.35
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function Plays an important role in the final stage of carbohydrate digestion
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action [RN:R00801 R06087] ALL_REAC R00801 R06087(G) > R00802 R06088(G)
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 13-32
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 36645 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P14410 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SUIS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >5484 bp
ATGGCAAGAAAGAAATTTAGTGGATTGGAAATCTCTCTGATTGTCCTTTTTGTCATAGTT
ACTATAATAGCTATTGCCTTAATTGTTGTTTTAGCAACTAAGACACCTGCTGTTGATGAA
ATTAGTGATTCTACTTCAACTCCAGCTACTACTCGTGTGACTACAAATCCTTCTGATTCA
GGAAAATGTCCAAATGTGTTAAATGATCCTGTCAATGTGAGAATAAACTGCATTCCAGAA
CAATTCCCAACAGAGGGAATTTGTGCACAGAGAGGCTGCTGCTGGAGGCCGTGGAATGAC
TCTCTTATTCCTTGGTGCTTCTTCGTTGATAATCATGGTTATAACGTTCAAGACATGACA
ACAACAAGTATTGGAGTTGAAGCCAAATTAAACAGGATACCTTCACCTACACTATTTGGA
AATGACATCAACAGTGTTCTCTTCACAACTCAAAATCAGACACCCAATCGTTTCCGGTTC
AAGATTACTGATCCAAATAATAGAAGATATGAAGTTCCTCATCAGTATGTAAAAGAGTTT
ACTGGACCCACAGTTTCTGATACGTTGTATGATGTGAAGGTTGCCCAAAACCCATTTAGC
ATCCAAGTTATTAGGAAAAGCAACGGTAAAACTTTGTTTGACACCAGCATTGGTCCCTTA
GTGTACTCTGACCAGTACTTACAGATCTCAGCCCGTCTTCCAAGTGATTATATTTATGGT
ATTGGAGAACAAGTTCATAAGAGATTTCGTCATGATTTATCCTGGAAAACATGGCCAATT
TTTACTCGAGACCAACTTCCTGGTGATAATAATAATAATTTATACGGCCATCAAACATTC
TTTATGTGTATTGAAGATACATCTGGAAAGTCATTCGGTGTTTTTTTAATGAATAGCAAT
GCAATGGAGATTTTTATCCAGCCTACTCCAATAGTAACATATAGAGTTACCGGTGGCATT
CTGGATTTTTACATCCTTCTAGGAGATACACCAGAACAAGTAGTTCAACAGTATCAACAG
CTTGTTGGACTACCAGCAATGCCAGCATATTGGAATCTTGGATTCCAACTAAGTCGCTGG
AATTATAAGTCACTAGATGTAGTGAAAGAAGTGGTAAGGAGAAACCGGGAAGCTGGCATA
CCATTTGATACACAGGTCACTGATATTGACTACATGGAAGACAAGAAAGACTTTACTTAT
GATCAAGTTGCGTTTAACGGACTCCCTCAATTTGTGCAAGATTTGCATGACCATGGACAG
AAATATGTCATCATCTTGGACCCTGCAATTTCCATAGGTCGACGTGCCAATGGAACAACA
TATGCAACCTATGAGAGGGGAAACACACAACATGTGTGGATAAATGAGTCAGATGGAAGT
ACACCAATTATTGGAGAGGTATGGCCAGGATTAACAGTATACCCTGATTTCACTAATCCA
AACTGCATTGATTGGTGGGCAAATGAATGCAGTATTTTCCATCAAGAAGTGCAATATGAT
GGACTTTGGATTGACATGAATGAAGTTTCCAGCTTTATTCAAGGTTCAACAAAAGGATGT
AATGTAAACAAATTGAATTATCCACCGTTTACTCCTGATATTCTTGACAAACTCATGTAT
TCCAAAACAATTTGCATGGATGCTGTGCAGAACTGGGGTAAACAGTATGATGTTCATAGC
CTCTATGGATACAGCATGGCTATAGCCACAGAGCAAGCTGTACAAAAAGTTTTTCCTAAT
AAGAGAAGCTTCATTCTTACCCGCTCAACATTTGCTGGATCTGGAAGACATGCTGCTCAT
TGGTTAGGAGACAATACTGCTTCATGGGAACAAATGGAATGGTCTATAACTGGAATGCTG
GAGTTCAGTTTGTTTGGAATACCTTTGGTTGGAGCAGACATCTGTGGATTTGTGGCTGAA
ACCACAGAAGAACTTTGCAGAAGATGGATGCAACTTGGGGCATTTTATCCATTTTCCAGA
AACCATAATTCTGACGGATATGAACATCAGGATCCTGCATTTTTTGGGCAGAATTCACTT
TTGGTTAAATCATCAAGGCAGTATTTAACTATTCGCTACACCTTATTACCCTTCCTCTAC
ACTCTGTTTTATAAAGCCCATGTGTTTGGAGAAACAGTAGCAAGACCAGTTCTTCATGAG
TTTTATGAGGATACGAACAGCTGGATTGAGGACACTGAGTTTTTGTGGGGCCCTGCATTA
CTTATTACTCCTGTTCTAAAACAGGGAGCAGATACTGTGAGTGCCTACATCCCTGATGCT
ATTTGGTATGATTATGAATCTGGTGCAAAAAGGCCATGGAGGAAACAACGGGTTGATATG
TATCTTCCAGCAGACAAAATAGGATTACATCTTAGAGGAGGTTATATCATCCCCATTCAA
GAACCAGATGTAACAACAACAGCAAGCCGTAAGAATCCTCTAGGACTTATAGTCGCATTA
GGTGAAAACAACACAGCCAAAGGAGACTTTTTCTGGGATGATGGAGAAACTAAAGATACA
ATACAAAATGGCAACTACATATTATATACATTTTCAGTTTCTAATAACACATTAGATATT
GTGTGCACACATTCATCATATCAGGAAGGAACTACCTTAGCATTTCAGACTGTAAAAATC
CTTGGGTTGACAGACAGTGTTACAGAAGTTAGAGTGGCGGAAAATAATCAACCAATGAAC
GCTCATTCCAATTTCACTTATGATGCTTCTAACCAGGTTCTCCTAATTGCAGATCTCAAA
CTTAATCTTGGAAGAAACTTTAGTGTTCAATGGAATCAAATTTTCTCAGAAAATGAAAGA
TTTAATTGTTATCCAGATGCAGATTTGGCAACTGAACAAAAGTGCACACAACGTGGCTGT
GTATGGAGAACGGGTTCTTCTCTATCCAAAGCACCTGAGTGTTACTTTCCCAGACAAGAT
AACTCTTATTCAGTCAACTCAGCTCGCTATTCATCCATGGGTATAACAGCTGACCTCCAA
CTAAATACTGCAAATGCCAGAATAAAGTTACCTTCTGACCCCATCTCAACTCTTCGTGTG
GAGGTGAAATATCACAAAAATGATATGTTGCAGTTTAAGATTTATGATCCCCAAAAGAAG
AGATATGAAGTACCAGTACCGTTAAACATTCCAACCACCCCAATAAGTACTTATGAAGAC
AGACTTTATGATGTGGAAATCAAGGAAAATCCTTTTGGCATCCAGATTCGACGGAGAAGC
AGTGGAAGAGTCATTTGGGATTCTTGGCTGCCTGGATTTGCTTTTAATGACCAGTTCATT
CAAATATCGACTCGCCTGCCATCAGAATATATATATGGTTTTGGGGAAGTGGAACATACA
GCATTTAAGCGAGATCTGAACTGGAATACTTGGGGAATGTTCACAAGAGACCAACCCCCT
GGTTACAAACTTAATTCCTATGGATTTCATCCCTATTACATGGCTCTGGAAGAGGAGGGC
AATGCTCATGGTGTTTTCTTACTCAACAGCAATGCAATGGATGTTACATTCCAGCCAACT
CCTGCTCTAACTTACCGTACAGTTGGAGGGATCTTGGATTTTTATATGTTTTTGGGCCCA
ACTCCACAAGTTGCAACAAAGCAATACCATGAAGTAATTGGCCATCCAGTCATGCCAGCT
TATTGGGCTTTGGGATTCCAATTATGTCGTTATGGATATGCAAATACTTCAGAGGTTCGG
GAATTATATGACGCTATGGTGGCTGCTAACATCCCCTATGATGTTCAGTACACAGACATT
GACTACATGGAAAGGCAGCTAGACTTTACAATTGGTGAAGCATTCCAGGACCTTCCTCAG
TTTGTTGACAAAATAAGAGGAGAAGGAATGAGATACATTATTATCCTGGATCCAGCAATT
TCAGGAAATGAAACAAAGACTTACCCTGCATTTGAAAGAGGACAGCAGAATGATGTCTTT
GTCAAATGGCCAAACACCAATGACATTTGTTGGGCAAAGGTTTGGCCAGATTTGCCCAAC
ATAACAATAGATAAAACTCTAACGGAAGATGAAGCTGTTAATGCTTCCAGAGCTCATGTA
GCTTTCCCAGATTTCTTCAGGACTTCCACAGCAGAGTGGTGGGCCAGAGAAATTGTGGAC
TTTTACAATGAAAAGATGAAGTTTGATGGTTTGTGGATTGATATGAATGAGCCATCAAGT
TTTGTAAATGGAACAACTACTAATCAATGCAGAAATGACGAACTAAATTATCCACCTTAT
TTCCCAGAACTCACAAAAAGAACTGATGGATTACATTTCAGAACAATTTGCATGGAAGCT
GAGCAGATTCTTAGTGATGGAACATCAGTTTTGCATTACGATGTTCACAATCTCTATGGA
TGGTCACAGATGAAACCTACTCATGATGCATTGCAAAAGACAACTGGAAAAAGAGGGATT
GTAATTTCTCGTTCCACGTATCCTACTAGTGGACGATGGGGAGGACACTGGCTTGGAGAC
AACTATGCACGATGGGACAACATGGACAAATCAATCATTGGTATGATGGAATTTAGTCTG
TTTGGAATATCATATACTGGAGCAGACATCTGTGGTTTTTTCAACAACTCAGAATATCAT
CTCTGTACCCGCTGGATGCAACTTGGAGCATTTTATCCATACTCAAGGAATCACAACATT
GCAAATACTAGAAGACAAGATCCCGCTTCCTGGAATGAAACTTTTGCTGAAATGTCAAGG
AATATTCTAAATATTAGATACACCTTATTGCCCTATTTTTACACACAAATGCATGAAATT
CATGCTAATGGTGGCACTGTTATCCGACCCCTTTTGCATGAGTTCTTTGATGAAAAACCA
ACCTGGGATATATTCAAGCAGTTCTTATGGGGTCCAGCATTTATGGTTACCCCAGTACTG
GAACCTTATGTTCAAACTGTAAATGCCTACGTCCCCAATGCTCGGTGGTTTGACTACCAT
ACAGGCAAAGATATTGGCGTCAGAGGACAATTTCAAACATTTAATGCTTCTTATGACACA
ATAAACCTACATGTCCGTGGTGGTCACATCCTACCATGTCAAGAGCCAGCTCAAAACACA
TTTTACAGTCGACAAAAACACATGAAGCTCATTGTTGCTGCAGATGATAATCAGATGGCA
CAGGGTTCTCTGTTTTGGGATGATGGAGAGAGTATAGACACCTATGAAAGAGACCTATAT
TTATCTGTACAATTTAATTTAAACCAGACCACCTTAACAAGCACTATATTGAAGAGAGGT
TACATAAATAAAAGTGAAACGAGGCTTGGATCCCTTCATGTATGGGGGAAAGGAACTACT
CCTGTCAATGCAGTTACTCTAACGTATAACGGAAATAAAAATTCGCTTCCTTTTAATGAA
GACACTACCAACATGATATTACGTATTGATCTGACCACACACAATGTTACTCTAGAAGAA
CCAATAGAAATCAACTGGTCATGA
Enzyme 1 GenBank Gene ID X63597 Link Image
Enzyme 1 GeneCard ID SI Link Image
Enzyme 1 GenAtlas ID SI Link Image
Enzyme 1 HGNC ID HGNC:10856 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3q25.2-q26.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Chantret I, Lacasa M, Chevalier G, Ruf J, Islam I, Mantei N, Edwards Y, Swallow D, Rousset M: Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J. 1992 Aug 1;285 ( Pt 3):915-23. [PubMed Link Image]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Green F, Edwards Y, Hauri HP, Povey S, Ho MW, Pinto M, Swallow D: Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3. Gene. 1987;57(1):101-10. [PubMed Link Image]
  5. Gorvel JP, Ferrero A, Chambraud L, Rigal A, Bonicel J, Maroux S: Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon. Gastroenterology. 1991 Sep;101(3):618-25. [PubMed Link Image]
  6. Ouwendijk J, Moolenaar CE, Peters WJ, Hollenberg CP, Ginsel LA, Fransen JA, Naim HY: Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J Clin Invest. 1996 Feb 1;97(3):633-41. [PubMed Link Image]
  7. Jacob R, Zimmer KP, Schmitz J, Naim HY: Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme. J Clin Invest. 2000 Jul;106(2):281-7. [PubMed Link Image]
  8. Spodsberg N, Jacob R, Alfalah M, Zimmer KP, Naim HY: Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder. J Biol Chem. 2001 Jun 29;276(26):23506-10. Epub 2001 May 4. [PubMed Link Image]
  9. Ritz V, Alfalah M, Zimmer KP, Schmitz J, Jacob R, Naim HY: Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum. Gastroenterology. 2003 Dec;125(6):1678-85. [PubMed Link Image]
  10. Sander P, Alfalah M, Keiser M, Korponay-Szabo I, Kovacs JB, Leeb T, Naim HY: Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption. Hum Mutat. 2006 Jan;27(1):119. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5603
Enzyme 2 Name Glycogen debranching enzyme
Enzyme 2 Synonyms
  1. Glycogen debrancher
  2. 4-alpha-glucanotransferase
  3. Oligo-1,4-1,4-glucantransferase
  4. Amylo-alpha-1,6-glucosidase
  5. Amylo-1,6-glucosidase
  6. Dextrin 6-alpha-D-glucosidase
Enzyme 2 Gene Name AGL
Enzyme 2 Protein Sequence >Glycogen debranching enzyme
MGHSKQIRILLLNEMEKLEKTLFRLEQGYELQFRLGPTLQGKAVTVYTNYPFPGETFNRE
KFRSLDWENPTEREDDSDKYCKLNLQQSGSFQYYFLQGNEKSGGGYIVVDPILRVGADNH
VLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLE
LNPDFSRPNRKYTWNDVGQLVEKLKKEWNVICITDVVYNHTAANSKWIQEHPECAYNLVN
SPHLKPAWVLDRALWRFSCDVAEGKYKEKGIPALIENDHHMNSIRKIIWEDIFPKLKLWE
FFQVDVNKAVEQFRRLLTQENRRVTKSDPNQHLTIIQDPEYRRFGCTVDMNIALTTFIPH
DKGPAAIEECCNWFHKRMEELNSEKHRLINYHQEQAVNCLLGNVFYERLAGHGPKLGPVT
RKHPLVTRYFTFPFEEIDFSMEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYL
RRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYML
DAARNLQPNLYVVAELFTGSEDLDNVFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEP
VGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTIVSMACCASGSTRGY
DELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARCAISKLHQELGAKGFIQV
YVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEAR
TIERNTKPYRKDENSINGTPDITVEIREHIQLNESKIVKQAGVATKGPNEYIQEIEFENL
SPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASLASRLT
LAELNQILYRCESEEKEDGGGCYDIPNWSALKYAGLQGLMSVLAEIRPKNDLGHPFCNNL
RSGDWMIDYVSNRLISRSGTIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLD
TAWKQMSSFVQNGSTFVKHLSLGSVQLCGVGKFPSLPILSPALMDVPYRLNEITKEKEQC
CVSLAAGLPHFSSGIFRCWGRDTFIALRGILLITGRYVEARNIILAFAGTLRHGLIPNLL
GEGIYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPL
FEVIQEAMQKHMQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWM
DKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSKKNIFPYHEVTVKRHGKAI
KVSYDEWNRKIQDNFEKLFHVSEDPSDLNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPN
FTIAMVVAPELFTTEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLA
KGFNYHQGPEWLWPIGYFLRAKLYFSRLMGPETTAKTIVLVKNVLSRHYVHLERSPWKGL
PELTNENAQYCPFSCETQAWSIATILETLYDL
Enzyme 2 Number of Residues 1532
Enzyme 2 Molecular Weight 174762.3
Enzyme 2 Theoretical pI 6.74
Enzyme 2 GO Classification
Function
  • 4-alpha-glucanotransferase activity
  • amylo-alpha-1,6-glucosidase activity
  • binding
  • catalytic activity
  • cation binding
  • glycogen debranching enzyme activity
  • ion binding
Process
  • alcohol metabolic process
  • carbohydrate metabolic process
  • glucose metabolic process
  • glycogen biosynthetic process
  • glycogen metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation
Enzyme 2 Pathways
Enzyme 2 Reactions
  • Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin ALL_REAC (other) R02109 R06158(G)
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 6580116 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P35573 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GDE_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >4599 bp
ATGGGACACAGTAAACAGATTCGAATTTTACTTCTGAACGAAATGGAGAAACTGGAAAAG
ACCCTCTTCAGACTTGAACAAGGGTATGAGCTACAGTTCCGATTAGGCCCAACTTTACAG
GGAAAAGCAGTTACCGTGTATACAAATTACCCATTTCCTGGAGAAACATTTAATAGAGAA
AAATTCCGTTCTCTGGATTGGGAAAATCCAACAGAAAGAGAAGATGATTCTGATAAATAC
TGTAAACTTAATCTGCAACAATCTGGTTCATTTCAGTATTATTTCCTTCAAGGAAATGAG
AAAAGTGGTGGAGGTTACATAGTTGTGGACCCCATTTTACGTGTTGGTGCTGATAATCAT
GTGCTACCCTTGGACTGTGTTACTCTTCAGACATTTTTAGCTAAGTGTTTGGGACCTTTT
GATGAATGGGAAAGCAGACTTAGGGTTGCAAAAGAATCAGGCTACAACATGATTCATTTT
ACCCCATTGCAGACTCTTGGACTATCTAGGTCATGCTACTCCCTTGCCAATCAGTTAGAA
TTAAATCCTGACTTTTCAAGACCTAATAGAAAGTATACCTGGAATGATGTTGGACAGCTA
GTGGAAAAATTAAAAAAGGAATGGAATGTTATTTGTATTACTGATGTTGTCTACAATCAT
ACTGCTGCTAATAGTAAATGGATCCAGGAACATCCAGAATGTGCCTATAATCTTGTGAAT
TCTCCACACTTAAAACCTGCCTGGGTCTTAGACAGAGCACTTTGGCGTTTCTCCTGTGAT
GTTGCAGAAGGGAAATACAAAGAAAAGGGAATACCTGCTTTGATTGAAAATGATCACCAT
ATGAATTCCATCCGAAAAATAATTTGGGAGGATATTTTTCCAAAGCTTAAACTTTGGGAA
TTTTTCCAAGTAGATGTCAACAAAGCGGTTGAGCAATTTAGAAGACTTCTTACACAAGAA
AATAGGCGAGTAACCAAGTCTGATCCAAACCAACACCTTACGATTATTCAAGATCCTGAA
TACAGACGGTTTGGCTGTACTGTAGATATGAACATTGCACTAACGACTTTCATACCACAT
GACAAGGGGCCAGCAGCAATTGAAGAATGCTGTAATTGGTTTCATAAAAGAATGGAGGAA
TTAAATTCAGAGAAGCATCGACTCATTAACTATCATCAGGAACAGGCAGTTAATTGCCTT
TTGGGAAATGTGTTTTATGAACGACTGGCTGGCCATGGTCCAAAACTAGGACCTGTCACT
AGAAAGCATCCTTTAGTTACCAGGTATTTTACTTTCCCATTTGAAGAGATAGACTTCTCC
ATGGAAGAATCTATGATTCATCTGCCAAATAAAGCTTGTTTTCTGATGGCACACAATGGA
TGGGTAATGGGAGATGATCCTCTTCGAAACTTTGCTGAACCGGGTTCAGAAGTTTACCTA
AGGAGAGAACTTATTTGCTGGGGAGACAGTGTTAAATTACGCTATGGGAATAAACCAGAG
GACTGTCCTTATCTCTGGGCACACATGAAAAAATACACTGAAATAACTGCAACTTATTTC
CAGGGAGTACGTCTTGATAACTGCCACTCAACACCTCTTCACGTAGCTGAGTACATGTTG
GATGCTGCTAGGAATTTGCAACCCAATTTATATGTAGTAGCTGAACTGTTCACAGGAAGT
GAAGATCTGGACAATGTCTTTGTTACTAGACTGGGCATTAGTTCCTTAATAAGAGAGGCA
ATGAGTGCATATAATAGTCATGAAGAGGGCAGATTAGTTTACCGATATGGAGGAGAACCT
GTTGGATCCTTTGTTCAGCCCTGTTTGAGGCCTTTAATGCCAGCTATTGCACATGCCCTG
TTTATGGATATTACGCATGATAATGAGTGTCCTATTGTGCATAGATCAGCGTATGATGCT
CTTCCAAGTACTACAATTGTTTCTATGGCATGTTGTGCTAGTGGAAGTACAAGAGGCTAT
GATGAATTAGTGCCTCATCAGATTTCAGTGGTTTCTGAAGAACGGTTTTACACTAAGTGG
AATCCTGAAGCATTGCCTTCAAACACAGGTGAAGTTAATTTCCAAAGCGGCATTATTGCA
GCCAGGTGTGCTATCAGTAAACTTCATCAGGAGCTTGGAGCCAAGGGTTTTATTCAGGTG
TATGTGGATCAAGTTGATGAAGACATAGTGGCAGTAACAAGACACTCACCTAGCATCCAT
CAGTCTGTTGTGGCTGTATCTAGAACTGCTTTCAGGAATCCCAAGACTTCATTTTACAGC
AAGGAAGTGCCTCAAATGTGCATCCCTGGCAAAATTGAAGAAGTAGTTCTTGAAGCTAGA
ACTATTGAGAGAAACACGAAACCTTATAGGAAGGATGAGAATTCAATCAATGGAACACCA
GATATCACAGTAGAAATTAGAGAACATATTCAGCTTAATGAAAGTAAAATTGTTAAACAA
GCTGGAGTTGCCACAAAAGGGCCCAATGAATATATTCAAGAAATAGAATTTGAAAACTTG
TCTCCAGGAAGTGTTATTATATTCAGAGTTAGTCTTGATCCACATGCACAAGTCGCTGTT
GGAATTCTTCGAAATCATCTGACACAATTCAGTCCTCACTTTAAATCTGGCAGCCTAGCT
GTTGACAATGCAGATCCTATATTAAAAATTCCTTTTGCTTCTCTTGCCTCCAGATTAACT
TTGGCTGAGCTAAATCAGATCCTTTACCGATGTGAATCAGAAGAAAAGGAAGATGGTGGA
GGGTGCTATGACATACCAAACTGGTCAGCCCTTAAATATGCAGGTCTTCAAGGTTTAATG
TCTGTATTGGCAGAAATAAGACCAAAGAATGACTTGGGGCATCCTTTTTGTAATAATTTG
AGATCTGGAGATTGGATGATTGACTATGTCAGTAACCGGCTTATTTCACGATCAGGAACT
ATTGCTGAAGTTGGTAAATGGTTGCAGGCTATGTTCTTCTACCTGAAGCAGATCCCACGT
TACCTTATCCCATGTTACTTTGATGCTATATTAATTGGTGCATATACCACTCTTCTGGAT
ACAGCATGGAAGCAGATGTCAAGCTTTGTTCAGAATGGTTCAACCTTTGTGAAACACCTT
TCATTGGGTTCAGTTCAACTGTGTGGAGTAGGAAAATTCCCTTCCCTGCCAATTCTTTCA
CCTGCCCTAATGGATGTACCTTATAGGTTAAATGAGATCACAAAAGAAAAGGAGCAATGT
TGTGTTTCTCTAGCTGCAGGCTTACCTCATTTTTCTTCTGGTATTTTCCGCTGCTGGGGA
AGGGATACTTTTATTGCACTTAGAGGTATACTGCTGATTACTGGACGCTATGTAGAAGCC
AGGAATATTATTTTAGCATTTGCGGGTACCCTGAGGCATGGTCTCATTCCTAATCTACTG
GGTGAAGGAATTTATGCCAGATACAATTGTCGGGATGCTGTGTGGTGGTGGCTGCAGTGT
ATCCAGGATTACTGTAAAATGGTTCCAAATGGTCTAGACATTCTCAAGTGCCCAGTTTCC
AGAATGTATCCTACAGATGATTCTGCTCCTTTGCCTGCTGGCACACTGGATCAGCCATTG
TTTGAAGTCATACAGGAAGCAATGCAAAAACACATGCAGGGCATACAGTTCCGAGAAAGG
AATGCTGGTCCCCAGATAGATCGAAACATGAAGGACGAAGGTTTTAATATAACTGCAGGA
GTTGATGAAGAAACAGGATTTGTTTATGGAGGAAATCGTTTCAATTGTGGCACATGGATG
GATAAAATGGGAGAAAGTGACAGAGCTAGAAACAGAGGAATCCCAGCCACACCAAGAGAT
GGGTCTGCTGTGGAAATTGTGGGCCTGAGTAAATCTGCTGTTCGCTGGTTGCTGGAATTA
TCCAAAAAAAATATTTTCCCTTATCATGAAGTCACAGTAAAAAGACATGGAAAGGCTATA
AAGGTCTCATATGATGAGTGGAACAGAAAAATACAAGACAACTTTGAAAAGCTATTTCAT
GTTTCCGAAGACCCTTCAGATTTAAATGAAAAGCATCCAAATCTGGTTCACAAACGTGGC
ATATACAAAGATAGTTATGGAGCTTCAAGTCCTTGGTGTGACTATCAGCTCAGGCCTAAT
TTTACCATAGCAATGGTTGTGGCCCCTGAGCTCTTTACTACAGAAAAAGCATGGAAAGCT
TTGGAGATTGCAGAAAAAAAATTGCTTGGTCCCCTTGGCATGAAAACTTTAGATCCAGAT
GATATGGTTTACTGTGGAATTTATGACAATGCATTAGACAATGACAACTACAATCTTGCT
AAAGGTTTCAATTATCACCAAGGACCTGAGTGGCTGTGGCCTATTGGGTATTTTCTTCGT
GCAAAATTATATTTTTCCAGATTGATGGGCCCGGAGACTACTGCAAAGACTATAGTTTTG
GTTAAAAATGTTCTTTCCCGACATTATGTTCATCTTGAGAGATCCCCTTGGAAAGGACTT
CCAGAACTGACCAATGAGAATGCCCAGTACTGTCCTTTCAGCTGTGAAACACAAGCCTGG
TCAATTGCTACTATTCTTGAGACACTTTATGATTTATAG
Enzyme 2 GenBank Gene ID AB035443 Link Image
Enzyme 2 GeneCard ID AGL Link Image
Enzyme 2 GenAtlas ID AGL Link Image
Enzyme 2 HGNC ID HGNC:321 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Yang BZ, Ding JH, Enghild JJ, Bao Y, Chen YT: Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme. J Biol Chem. 1992 May 5;267(13):9294-9. [PubMed Link Image]
  2. Bao Y, Dawson TL Jr, Chen YT: Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region. Genomics. 1996 Dec 1;38(2):155-65. [PubMed Link Image]
  3. Bao Y, Yang BZ, Dawson TL Jr, Chen YT: Isolation and nucleotide sequence of human liver glycogen debranching enzyme mRNA: identification of multiple tissue-specific isoforms. Gene. 1997 Sep 15;197(1-2):389-98. [PubMed Link Image]
  4. Okubo M, Horinishi A, Takeuchi M, Suzuki Y, Sakura N, Hasegawa Y, Igarashi T, Goto K, Tahara H, Uchimoto S, Omichi K, Kanno H, Hayasaka K, Murase T: Heterogeneous mutations in the glycogen-debranching enzyme gene are responsible for glycogen storage disease type IIIa in Japan. Hum Genet. 2000 Jan;106(1):108-15. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  8. Cheng A, Zhang M, Gentry MS, Worby CA, Dixon JE, Saltiel AR: A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev. 2007 Oct 1;21(19):2399-409. [PubMed Link Image]
  9. Okubo M, Kanda F, Horinishi A, Takahashi K, Okuda S, Chihara K, Murase T: Glycogen storage disease type IIIa: first report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient. Hum Mutat. 1999 Dec;14(6):542-3. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7564
Enzyme 3 Name Alpha-amylase 1
Enzyme 3 Synonyms
  1. 1,4-alpha-D-glucan glucanohydrolase 1
  2. Salivary alpha-amylase
Enzyme 3 Gene Name AMY1A
Enzyme 3 Protein Sequence >Alpha-amylase 1
MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGL
LDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Enzyme 3 Number of Residues 511
Enzyme 3 Molecular Weight 57767.5
Enzyme 3 Theoretical pI 6.92
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides
Enzyme 3 Pathways
Enzyme 3 Reactions
  • Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units ALL_REAC (other) R02108 R06209(G)
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-15
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P04745 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AMY1_HUMAN Link Image
Enzyme 3 PDB ID 1MFV Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1536 bp
ATGAAGCTCTTTTGGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCTCAAAT
ACACAACAAGGACGAACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCCAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCCATTCACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGCAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTGTGGTAAT
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTTAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAACTATAATGATGCTACTCAGGTCAGAGATTGTCGTCTGTCTGGTCTT
CTCGATCTTGCACTGGGGAAGGATTATGTGCGTTCTAAGATTGCCGAATATATGAACCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGAATTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCGGAAGGT
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGTAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACTTAAAGAACTGGGGAGAAGGTTGGGGT
TTCATGCCTTCTGACAGAGCGCTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGCGCTGGAGGAGCCTCTATACTTACCTTCTGGGATGCTAGGCTGTACAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTATGGATTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGATATTTTGAAAATGGAAAAGATGTTAATGATTGGGTTGGGCCACCAAATGATAATGGA
GTAACTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTAATTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAACTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGACATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAACTGCACAGGCATT
AAAATCTACGTTTCTGATGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAAGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTGTAA
Enzyme 3 GenBank Gene ID AK292341 Link Image
Enzyme 3 GeneCard ID AMY1A Link Image
Enzyme 3 GenAtlas ID AMY1A Link Image
Enzyme 3 HGNC ID HGNC:474 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Nishide T, Nakamura Y, Emi M, Yamamoto T, Ogawa M, Mori T, Matsubara K: Primary structure of human salivary alpha-amylase gene. Gene. 1986;41(2-3):299-304. [PubMed Link Image]
  2. Nishide T, Emi M, Nakamura Y, Matsubara K: Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] Gene. 1984 May;28(2):263-70. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed Link Image]
  7. Handy DE, Larsen SH, Karn RC, Hodes ME: Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1. Mol Biol Med. 1987 Jun;4(3):145-55. [PubMed Link Image]
  8. Bank RA, Hettema EH, Arwert F, Amerongen AV, Pronk JC: Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. Electrophoresis. 1991 Jan;12(1):74-9. [PubMed Link Image]
  9. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed Link Image]
  10. Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ: Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity. Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. [PubMed Link Image]
  11. Ramasubbu N, Ragunath C, Mishra PJ: Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. J Mol Biol. 2003 Jan 31;325(5):1061-76. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7565
Enzyme 4 Name Pancreatic alpha-amylase
Enzyme 4 Synonyms
  1. PA
  2. 1,4-alpha-D-glucan glucanohydrolase
Enzyme 4 Gene Name AMY2A
Enzyme 4 Protein Sequence >Pancreatic alpha-amylase
MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGL
LDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Enzyme 4 Number of Residues 511
Enzyme 4 Molecular Weight 57706.5
Enzyme 4 Theoretical pI 7.05
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 4 General Function Involved in catalytic activity
Enzyme 4 Specific Function Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides
Enzyme 4 Pathways
Enzyme 4 Reactions
  • Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units ALL_REAC (other) R02108 R06209(G)
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 529397 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P04746 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AMYP_HUMAN Link Image
Enzyme 4 PDB ID 1B2Y Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1536 bp
ATGAAGTTCTTTCTGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCCCAAAT
ACACAACAAGGACGGACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCGAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCAATTTACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGTAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTGTGGTAAC
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTCAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAATTACAATGATGCTACTCAGGTCAGAGATTGTCGTCTGACTGGTCTT
CTTGATCTTGCACTGGAGAAGGATTACGTGCGTTCTAAGATTGCCGAATATATGAACCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGACTTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCTGCAGGA
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGTAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACTTAAAGAACTGGGGAGAAGGTTGGGGT
TTCGTACCTTCTGACAGAGCGCTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGGGCTGGAGGAGCCTCTATTCTTACCTTCTGGGATGCTAGGCTGTACAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTACGGATTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGACAGTTTCAAAATGGAAACGATGTTAACGATTGGGTTGGGCCACCAAATAATAATGGA
GTAATTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTATTTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAATTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGTCATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAATTGCACAGGCATT
AAAATTTACGTTTCTGATGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAAGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTGTAA
Enzyme 4 GenBank Gene ID M28443 Link Image
Enzyme 4 GeneCard ID AMY2A Link Image
Enzyme 4 GenAtlas ID AMY2A Link Image
Enzyme 4 HGNC ID HGNC:477 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nishide T, Emi M, Nakamura Y, Matsubara K: Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] Gene. 1984 May;28(2):263-70. [PubMed Link Image]
  2. Horii A, Emi M, Tomita N, Nishide T, Ogawa M, Mori T, Matsubara K: Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene. Gene. 1987;60(1):57-64. [PubMed Link Image]
  3. Wise RJ, Karn RC, Larsen SH, Hodes ME, Gardell SJ, Rutter WJ: A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A. Mol Biol Med. 1984 Oct;2(5):307-22. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR: Human pancreatic amylase is encoded by two different genes. Nucleic Acids Res. 1988 May 25;16(10):4724. [PubMed Link Image]
  6. Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed Link Image]
  7. Qian M, Haser R, Buisson G, Duee E, Payan F: The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution. Biochemistry. 1994 May 24;33(20):6284-94. [PubMed Link Image]
  8. Brayer GD, Luo Y, Withers SG: The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. Protein Sci. 1995 Sep;4(9):1730-42. [PubMed Link Image]
  9. Rydberg EH, Sidhu G, Vo HC, Hewitt J, Cote HC, Wang Y, Numao S, MacGillivray RT, Overall CM, Brayer GD, Withers SG: Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Protein Sci. 1999 Mar;8(3):635-43. [PubMed Link Image]
  10. Brayer GD, Sidhu G, Maurus R, Rydberg EH, Braun C, Wang Y, Nguyen NT, Overall CM, Withers SG: Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry. 2000 Apr 25;39(16):4778-91. [PubMed Link Image]
  11. Numao S, Maurus R, Sidhu G, Wang Y, Overall CM, Brayer GD, Withers SG: Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase. Biochemistry. 2002 Jan 8;41(1):215-25. [PubMed Link Image]
  12. Rydberg EH, Li C, Maurus R, Overall CM, Brayer GD, Withers SG: Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids. Biochemistry. 2002 Apr 2;41(13):4492-502. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7629
Enzyme 5 Name Alpha-amylase 2B
Enzyme 5 Synonyms
  1. 1,4-alpha-D-glucan glucanohydrolase 2B
  2. Carcinoid alpha-amylase
Enzyme 5 Gene Name AMY2B
Enzyme 5 Protein Sequence >Alpha-amylase 2B
MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLVGL
LDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Enzyme 5 Number of Residues 511
Enzyme 5 Molecular Weight 57709.5
Enzyme 5 Theoretical pI 7.10
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 5 General Function Involved in catalytic activity
Enzyme 5 Specific Function Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units ALL_REAC (other) R02108 R06209(G)
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 193785276 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P19961 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AMY2B_HUMAN Link Image
Enzyme 5 PDB ID 1B2Y Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1536 bp
ATGAAGTTCTTTCTGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCCCAAAT
ACACAACAAGGACGGACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCCAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCAATTCACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGTAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTCTGGTAAT
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTTAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAACTACAATGATGCTACTCAGGTCAGAGATTGTCGTCTGGTTGGTCTT
CTTGATCTTGCACTGGAGAAAGATTATGTGCGTTCCAAGATTGCCGAATATATGAATCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGACTTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCTGCAGGA
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGAAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACCTAAAGAACTGGGGAGAAGGTTGGGGT
TTCATGCCTTCTGACAGAGCACTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGGGCTGGAGGAGCCTCTATTCTTACCTTCTGGGATGCTAGGCTGTATAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTATGGTTTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGACAGTTTCAAAATGGAAACGATGTTAATGATTGGGTTGGGCCACCAAATAATAATGGA
GTAATTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTAATTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAACTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGACATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAATTGCACAGGCATT
AAAATCTACGTTTCTGACGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAGGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTATAA
Enzyme 5 GenBank Gene ID AK127047 Link Image
Enzyme 5 GeneCard ID AMY2B Link Image
Enzyme 5 GenAtlas ID AMY2B Link Image
Enzyme 5 HGNC ID HGNC:478 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p21
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Tomita N, Horii A, Doi S, Yokouchi H, Shiosaki K, Higashiyama M, Matsuura N, Ogawa M, Mori T, Matsubara K: A novel type of human alpha-amylase produced in lung carcinoid tumor. Gene. 1989 Mar 15;76(1):11-8. [PubMed Link Image]
  2. Yokouchi H, Horii A, Emi M, Tomita N, Doi S, Ogawa M, Mori T, Matsubara K: Cloning and characterization of a third type of human alpha-amylase gene, AMY2B. Gene. 1990 Jun 15;90(2):281-6. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed Link Image]
  6. Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR: Human pancreatic amylase is encoded by two different genes. Nucleic Acids Res. 1988 May 25;16(10):4724. [PubMed Link Image]
  7. Omichi K, Hase S: Identification of the characteristic amino-acid sequence for human alpha-amylase encoded by the AMY2B gene. Biochim Biophys Acta. 1993 Dec 8;1203(2):224-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 8603
Enzyme 6 Name Maltase-glucoamylase, intestinal
Enzyme 6 Synonyms
  1. Maltase
  2. Alpha-glucosidase
  3. Glucoamylase
  4. Glucan 1,4-alpha-glucosidase
Enzyme 6 Gene Name MGAM
Enzyme 6 Protein Sequence >Maltase-glucoamylase, intestinal
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTP
DPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWN
PQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTS
NRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDS
SIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLY
GAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVV
QEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDER
RDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNS
SDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGS
VSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKT
VFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICG
FALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLL
PYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAY
VPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGL
IIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFN
EIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRD
EEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADIS
LKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEG
QLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHR
SYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPL
PALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIA
SLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAI
SGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYV
AFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDAS
LNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEV
TGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFF
QDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLY
TLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRA
RWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIAL
DDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIE
IWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
Enzyme 6 Number of Residues 1857
Enzyme 6 Molecular Weight 209850.8
Enzyme 6 Theoretical pI 5.17
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 6 General Function Involved in catalytic activity
Enzyme 6 Specific Function May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing
Enzyme 6 Pathways
Enzyme 6 Reactions
  • Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of D-glucose ALL_REAC (other) R00028 R00801 R00802 R06084(G) R06087(G) R06088(G) INHIBITOR Castanospermine [CPD:C02256]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 14-34
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 221316699 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O43451 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name MGA_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >5574 bp
ATGGCAAGAAAGAAGCTGAAAAAATTTACTACTTTGGAGATTGTGCTCAGTGTTCTTCTG
CTTGTGTTGTTTATCATCAGTATTGTTCTAATTGTGCTTTTAGCCAAAGAGTCACTGAAA
TCAACAGCCCCAGATCCTGGGACAACTGGTACCCCAGATCCTGGGACAACTGGTACCCCA
GATCCTGGAACAACTGGTACCACACATGCTAGGACAACGGGTCCCCCAGATCCTGGAACA
ACTGGTACCACTCCTGTTTCTGCTGAATGTCCAGTGGTAAATGAATTGGAACGAATTAAT
TGCATCCCTGACCAGCCGCCAACAAAGGCCACATGTGACCAACGTGGCTGTTGCTGGAAT
CCCCAGGGAGCTGTAAGTGTTCCCTGGTGCTACTATTCCAAGAATCATAGCTACCATGTA
GAGGGCAACCTTGTCAACACAAATGCAGGATTCACAGCCCGGTTGAAAAATCTGCCTTCT
TCACCAGTGTTTGGAAGCAATGTTGACAATGTTCTTCTCACAGCAGAATATCAGACATCT
AATCGTTTCCACTTTAAGTTGACTGACCAAACCAATAACAGGTTTGAAGTGCCCCACGAA
CACGTGCAGTCCTTCAGTGGAAATGCTGCTGCTTCTTTGACCTACCAAGTTGAAATCTCC
AGACAGCCATTTAGCATCAAAGTGACCAGAAGAAGCAACAATCGTGTTTTGTTTGACTCG
AGCATTGGGCCCCTACTGTTTGCTGACCAGTTCTTGCAGCTCTCCACTCGACTGCCTAGC
ACTAACGTGTATGGCCTGGGAGAGCATGTGCACCAGCAGTATCGGCATGATATGAATTGG
AAGACCTGGCCCATATTTAACAGAGACACAACTCCCAATGGAAACGGAACTAATTTGTAT
GGTGCGCAGACATTCTTCTTGTGCCTTGAAGATGCTAGTGGATTGTCCTTTGGGGTGTTT
CTGATGAACAGCAATGCCATGGAGGTTGTCCTTCAGCCTGCGCCAGCCATCACTTACCGC
ACCATTGGGGGCATTCTCGACTTCTATGTGTTCTTGGGAAACACTCCAGAGCAAGTTGTT
CAAGAATATCTAGAGCTCATTGGGCGGCCAGCCCTTCCCTCCTACTGGGCGCTTGGATTT
CACCTCAGTCGTTACGAATATGGAACCTTAGACAACATGAGGGAAGTCGTGGAGAGAAAT
CGCGCAGCACAGCTCCCTTATGATGTTCAGCATGCTGATATTGATTATATGGATGAGAGA
AGGGACTTCACTTATGATTCAGTGGATTTTAAAGGCTTCCCTGAATTTGTCAACGAGTTA
CACAATAATGGACAGAAGCTTGTCATCATTGTGGATCCAGCCATCTCCAACAACTCTTCC
TCAAGTAAACCCTATGGCCCATATGACAGGGGTTCAGATATGAAGATATGGGTGAATAGT
TCAGATGGAGTGACTCCACTCATTGGGGAGGTCTGGCCTGGACAAACTGTGTTTCCTGAT
TATACCAATCCCAACTGTGCTGTTTGGTGGACAAAGGAATTTGAGCTTTTTCACAATCAA
GTAGAGTTTGATGGAATCTGGATTGATATGAATGAAGTCTCCAACTTTGTTGATGGTTCG
GTCTCAGGATGTTCCACAAACAACCTAAATAATCCCCCATTCACTCCCAGAATCCTGGAT
GGGTACCTGTTCTGCAAGACTCTCTGTATGGATGCAGTGCAGCACTGGGGCAAGCAGTAT
GACATTCACAATCTGTATGGCTACTCCATGGCGGTCGCCACAGCAGAAGCTGCCAAGACT
GTGTTCCCTAATAAGAGAAGCTTCATTCTGACCCGTTCTACCTTTGCGGGCTCTGGCAAG
TTTGCAGCACATTGGTTAGGAGACAACACTGCCACCTGGGATGACCTGAGATGGTCCATC
CCTGGCGTGCTTGAGTTCAACCTTTTTGGCATCCCAATGGTGGGTCCTGACATATGTGGC
TTTGCTTTGGACACCCCTGAGGAGCTCTGTAGGCGGTGGATGCAGTTGGGTGCATTTTAT
CCGTTTTCTAGAAATCACAATGGCCAAGGCTACAAGGACCAGGATCCTGCCTCCTTTGGA
GCTGACTCCCTGCTGTTGAATTCCTCCAGGCACTACCTTAACATCCGCTATACTCTATTG
CCCTACCTATACACCCTCTTCTTCCGTGCTCACAGCCGAGGGGACACGGTGGCCAGGCCC
CTTTTGCATGAGTTCTACGAGGACAACAGCACTTGGGATGTGCACCAACAGTTCTTATGG
GGGCCCGGCCTCCTCATCACTCCAGTTCTGGATGAAGGTGCAGAGAAAGTGATGGCATAT
GTGCCTGATGCTGTCTGGTATGACTACGAGACTGGGAGCCAAGTGAGATGGAGGAAGCAA
AAAGTCGAGATGGAACTTCCTGGAGACAAAATTGGACTTCACCTTCGAGGAGGCTACATC
TTCCCCACACAGCAGCCAAATACAACCACTCTGGCCAGTCGAAAGAACCCTCTTGGTCTT
ATCATTGCCCTAGATGAGAACAAAGAAGCAAAAGGAGAACTTTTCTGGGATAATGGGGAA
ACGAAGGATACTGTGGCCAATAAAGTGTATCTTTTATGTGAGTTTTCTGTCACTCAAAAC
CGCTTGGAGGTGAATATTTCACAATCAACCTACAAGGACCCCAATAATTTAGCATTTAAT
GAGATTAAAATTCTTGGGACGGAGGAACCTAGCAATGTTACAGTGAAACACAATGGTGTC
CCAAGTCAGACTTCTCCTACAGTCACTTATGATTCTAACCTGAAGGTTGCCATTATCACA
GATATTGATCTTCTCCTGGGAGAAGCATACACAGTGGAATGGAGCATAAAGATAAGGGAT
GAAGAAAAAATAGACTGTTACCCTGATGAGAATGGTGCTTCTGCCGAAAACTGCACTGCC
CGTGGCTGTATCTGGGAGGCATCCAATTCTTCTGGAGTCCCTTTTTGCTATTTTGTCAAC
GACCTATACTCTGTCAGTGATGTTCAGTATAATTCCCATGGGGCCACAGCTGACATCTCC
TTAAAGTCTTCCGTTTATGCCAATGCCTTCCCCTCCACACCCGTGAACCCCCTTCGCCTG
GATGTCACTTACCATAAGAATGAAATGCTGCAGTTCAAGATTTATGATCCCAACAAGAAT
CGGTATGAAGTTCCAGTCCCTCTGAACATACCCAGCATGCCATCCAGCACCCCTGAGGGT
CAACTCTATGATGTGCTCATTAAGAAGAATCCATTTGGGATTGAAATTCGCCGGAAGAGT
ACAGGCACTATAATTTGGGACTCTCAGCTCCTTGGCTTTACCTTCAGTGACATGTTTATC
CGCATCTCCACCCGCCTTCCCTCCAAGTACCTCTATGGCTTTGGGGAAACTGAGCACAGG
TCCTATAGGAGAGACTTGGAGTGGCACACTTGGGGGATGTTCTCCCGAGACCAGCCCCCA
GGGTACAAGAAGAATTCCTATGGTGTCCACCCCTACTACATGGGGCTGGAGGAGGACGGC
AGTGCCCATGGAGTGCTCCTGCTGAACAGCAATGCCATGGATGTGACGTTCCAGCCCCTG
CCTGCCTTGACATACCGCACCACAGGGGGAGTTCTGGACTTTTATGTGTTCTTGGGGCCG
ACTCCAGAGCTTGTCACCCAGCAGTACACTGAGTTGATTGGCCGGCCTGTGATGGTACCT
TACTGGTCTTTGGGGTTCCAGCTGTGTCGCTATGGCTACCAGAATGACTCTGAGATCGCC
AGCTTGTATGATGAGATGGTGGCTGCCCAGATCCCTTATGATGTGCAGTACTCAGACATC
GACTACATGGAGCGGCAGCTGGACTTCACCCTCAGCCCCAAGTTTGCTGGGTTTCCAGCT
CTGATCAATCGCATGAAGGCTGATGGGATGCGGGTCATCCTCATTCTGGATCCAGCCATT
TCTGGCAATGAGACACAGCCTTATCCTGCCTTCACTCGGGGCGTGGAGGATGACGTCTTC
ATCAAATACCCAAATGATGGAGACATTGTCTGGGGAAAGGTCTGGCCTGATTTTCCTGAT
GTTGTTGTGAATGGGTCTCTAGACTGGGACAGCCAAGTGGAGCTATATCGAGCTTATGTG
GCCTTCCCAGACTTTTTCCGTAATTCAACTGCCAAGTGGTGGAAGAGGGAAATAGAAGAA
CTATACAACAATCCACAGAATCCAGAGAGGAGCTTGAAGTTTGATGGCATGTGGATTGAT
ATGAATGAACCATCAAGCTTCGTGAATGGGGCAGTTTCTCCAGGCTGCAGGGACGCCTCT
CTGAACCACCCTCCCTACATGCCACATTTGGAGTCCAGGGACAGGGGCCTGAGCAGCAAG
ACCCTTTGTATGGAGAGTCAGCAGATCCTCCCAGACGGCTCCCTGGTGCAGCACTACAAC
GTGCACAACCTGTATGGGTGGTCCCAGACCAGACCCACATACGAAGCCGTGCAGGAGGTG
ACGGGACAGCGAGGGGTCGTCATCACCCGCTCCACATTTCCCTCTTCTGGCCGCTGGGCA
GGACATTGGCTGGGAGACAACACGGCCGCATGGGATCAGCTGAAGAAGTCTATCATTGGC
ATGATGGAGTTCAGCCTCTTCGGCATATCCTATACGGGAGCAGATATCTGTGGGTTCTTT
CAAGATGCTGAATATGAGATGTGTGTTCGCTGGATGCAGCTGGGGGCCTTTTACCCCTTC
TCAAGAAACCACAACACCATTGGGACCAGGAGACAAGACCCTGTGTCCTGGGATGTTGCT
TTTGTGAATATTTCCAGAACTGTCCTGCAGACCAGATACACCCTGTTGCCATATCTGTAT
ACCTTGATGCATAAGGCCCACACGGAGGGCGTCACTGTTGTGCGGCCTCTGCTCCATGAG
TTTGTGTCAGACCAGGTGACATGGGACATAGACAGTCAGTTCCTGCTGGGCCCAGCCTTC
CTGGTCAGCCCTGTCCTGGAGCGTAATGCCAGAAATGTCACTGCATATTTCCCTAGAGCC
CGCTGGTATGATTACTACACGGGTGTGGATATTAATGCAAGAGGAGAGTGGAAGACCTTG
CCAGCCCCTCTTGACCACATTAATCTTCATGTCCGTGGGGGCTACATCCTGCCCTGGCAA
GAGCCTGCACTGAACACCCACTTAAGCCGCCAGAAATTCATGGGCTTCAAAATTGCCTTG
GATGATGAAGGAACTGCTGGGGGCTGGCTCTTCTGGGATGATGGGCAAAGCATTGATACC
TATGGGAAAGGACTCTATTACTTGGCCAGCTTTTCTGCCAGCCAGAATACGATGCAAAGC
CATATAATTTTCAACAATTACATCACTGGTACAAATCCTTTGAAACTGGGCTACATTGAA
ATCTGGGGAGTGGGCAGTGTCCCCGTTACCAGTGTCAGCATCTCTGTGAGTGGCATGGTC
ATAACACCCTCCTTCAACAATGACCCCACGACACAGGTATTAAGCATCGATGTGACTGAC
AGAAACATCAGCCTACATAATTTTACTTCATTGACGTGGATAAGCACTCTGTGA
Enzyme 6 GenBank Gene ID NM_004668.2 Link Image
Enzyme 6 GeneCard ID MGAM Link Image
Enzyme 6 GenAtlas ID MGAM Link Image
Enzyme 6 HGNC ID HGNC:7043 Link Image
Enzyme 6 Chromosome Location 7
Enzyme 6 Locus 7q34
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E: Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem. 1998 Jan 30;273(5):3076-81. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Naim HY, Sterchi EE, Lentze MJ: Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J Biol Chem. 1988 Dec 25;263(36):19709-17. [PubMed Link Image]
  5. Danielsen EM: Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO J. 1987 Oct;6(10):2891-6. [PubMed Link Image]
  6. Sim L, Quezada-Calvillo R, Sterchi EE, Nichols BL, Rose DR: Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. J Mol Biol. 2008 Jan 18;375(3):782-92. Epub 2007 Nov 1. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16095
Enzyme 7 Name Lysozyme-like protein 1
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name LYZL1
Enzyme 7 Protein Sequence >Lysozyme-like protein 1
MKAAGILTLIGCLVTGAESKIYTRCKLAKIFSRAGLDNYWGFSLGNWICMAYYESGYNTT
AQTVLDDGSIDYGIFQINSFAWCRRGKLKENNHCHVACSALITDDLTDAIICARKIVKET
QGMNYWQGWKKHCEGRDLSEWKKGCEVS
Enzyme 7 Number of Residues 148
Enzyme 7 Molecular Weight 16654.0
Enzyme 7 Theoretical pI 8.14
Enzyme 7 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • lysozyme activity
Process
  • catabolic process
  • cell wall macromolecule catabolic process
  • metabolic process
Component
Enzyme 7 General Function Involved in lysozyme activity
Enzyme 7 Specific Function Hydrolysis of (1->4)-beta-linkages between N- acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-19
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 37182510 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q6UWQ5 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name LYZL1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >447 bp
ATGAAGGCTGCGGGCATTCTGACCCTCATTGGCTGCCTGGTCACAGGCGCCGAGTCCAAA
ATCTACACTCGTTGCAAACTGGCAAAAATATTCTCGAGGGCTGGCCTGGACAATTACTGG
GGCTTCAGCCTTGGAAACTGGATCTGCATGGCATATTATGAGAGCGGCTACAACACCACA
GCCCCGACGGTCCTGGATGACGGCAGCATCGACTATGGCATCTTCCAGATCAACAGCTTC
GCGTGGTGCAGACGCGGAAAGCTGAAGGAGAACAACCACTGCCATGTCGCCTGCTCAGCC
TTGATCACTGATGACCTCACAGATGCAATTATCTGTGCCAGGAAAATTGTTAAAGAGACA
CAAGGAATGAACTATTGGCAAGGCTGGAAGAAACATTGTGAGGGCAGAGACCTGTCCGAG
TGGAAAAAAGGCTGTGAGGTTTCCTAA
Enzyme 7 GenBank Gene ID AY358694 Link Image
Enzyme 7 GeneCard ID LYZL1 Link Image
Enzyme 7 GenAtlas ID LYZL1 Link Image
Enzyme 7 HGNC ID HGNC:30502 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 10p12.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16792
Enzyme 8 Name cDNA FLJ45104 fis, clone BRAWH3032930, highly similar to Alpha-amylase 2B (EC 3.2.1.1)
Enzyme 8 Synonyms
  1. SubName: HCG2028285, isoform CRA_a
Enzyme 8 Gene Name Not Available
Enzyme 8 Protein Sequence >cDNA FLJ45104 fis, clone BRAWH3032930, highly similar to Alpha-amylase 2B (EC 3.2.1.1)
MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLVGL
LDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
Enzyme 8 Number of Residues 511
Enzyme 8 Molecular Weight 57710
Enzyme 8 Theoretical pI 7.10
Enzyme 8 GO Classification
Function
  • alpha-amylase activity
  • amylase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • Endohydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides containing three or more 1,4-alpha-linked D-glucose units ALL_REAC (other) R02108 R06209(G)
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B3KXB7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B3KXB7_HUMAN Link Image
Enzyme 8 PDB ID 1B2Y Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK127047 Link Image
Enzyme 8 GeneCard ID B3KXB7 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs Not Available
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available