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Human Metabolome Database Version 2.5

 

Showing metabocard for Allysine (HMDB01263)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:40
Accession Number HMDB01263
Secondary Accession Numbers Not Available
Common Name Allysine
Description Allysine is a derivative of Lysine, used in the production of elastin and collagen. It is produced by the actions of the enzyme lysyl oxidase in the extracellular matrix and is essential in the crosslink formation that stabilizes collagen and elastin.
Synonyms
  1. 2-Amino-5-formylvalerate
  2. 2-Amino-5-formylvaleric acid
  3. 2-amino-hexanedioic acid semialdhyde
  4. 2-aminoadipate semialdehyde
  5. 2-aminoadipate-6-semialdehyde
  6. L-2-Aminoadipate 6-semialdehyde
  7. 5-formyl-Norvaline
  8. 6-oxo-L-norleucine
  9. 6-oxo-Norleucine
  10. Allysine
  11. alpha-Aminoadipic acid delta-semialdehyde
  12. alpha-Aminoadipic delta-semialdehyde
  13. alpha-Aminoadipic semialdehyde
  14. 2-aminoadipate 6-semialdehyde
  15. (2S)-2-amino-6-oxohexanoic acid
  16. L-Allysine
  17. L-6-oxonorleucine
  18. 2-amino-hexanedioate
  19. (2S)-2-amino-6-oxohexanoate
  20. 2-amino-hexanedioic acid
Chemical IUPAC Name 2-amino-6-oxo-hexanoic acid
Chemical Formula C6H11NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 145.156
Monoisotopic Molecular Weight 145.073898
Isomeric SMILES NC(CCCC=O)C(O)=O
Canonical SMILES NC(CCCC=O)C(O)=O
KEGG Compound ID C01475 Link Image
BioCyc ID ALLYSINE Link Image
BiGG ID 1445244 Link Image
Wikipedia Link Allysine Link Image
NuGOwiki Link HMDB01263 Link Image
Metagene Link HMDB01263 Link Image
METLIN ID 6118 Link Image
PubChem Compound 207 Link Image
PubChem Substance 2125 Link Image
ChEBI ID 17027; 17917 Link Image
CAS Registry Number 1962-83-0
InChI Identifier InChI=1/C6H11NO3/c7-5(6(9)10)3-1-2-4-8/h4-5H,1-3,7H2,(H,9,10)
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 49.4 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.20 [Predicted by ALOGPS]; -2.6 [Predicted by PubChem via XLOGP] 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
  • Cytoplasm
  • mitochondria
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
Lysine Degradation SMP00037 Link Image map00310 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Alpha-aminoadipic semialdehyde synthase, mitochondrial
  2. Acyl-CoA synthetase family member 4
Enzyme 1 [top]
Enzyme 1 ID 6133
Enzyme 1 Name Alpha-aminoadipic semialdehyde synthase, mitochondrial
Enzyme 1 Synonyms
  1. LKR/SDH
  2. Lysine ketoglutarate reductase
  3. LKR
  4. LOR
  5. Saccharopine dehydrogenase
  6. SDH
Enzyme 1 Gene Name AASS
Enzyme 1 Protein Sequence >Alpha-aminoadipic semialdehyde synthase, mitochondrial 
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQ
PSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANM
GLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM
HIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPC
EYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIA
PYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTG
GSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLY
PYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTR
RKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKL
GFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGE
LGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMN
VMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTL
LRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLK
EAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRD
SFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFS
KEIYGPILERIKAEGIIYTTQSTIKP
Enzyme 1 Number of Residues 926
Enzyme 1 Molecular Weight 102130.9
Enzyme 1 Theoretical pI 6.62
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively
Enzyme 1 Pathways
Enzyme 1 Reactions
  • N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ [RN:R02313]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q9UDR5 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AASS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2781 bp 
ATGCTGCAAGTACATAGGACTGGACTGGGCAGGCTGGGGGTCAGCCTCTCCAAGGGTCTT
CACCACAAAGCTGTGTTGGCCGTCCGGAGGGAGGATGTGAACGCCTGGGAGAGAAGGGCC
CCGCTAGCTCCCAAGCACATCAAAGGCATCACCAATCTGGGATACAAGGTCTTGATACAG
CCTTCGAATCGGCGGGCCATTCATGATAAGGACTATGTCAAAGCTGGTGGCATTCTTCAG
GAGGATATTTCTGAAGCTTGTCTAATTTTAGGAGTTAAAAGACCTCCAGAGGAAAAATTA
ATGTCCAGGAAGACTTATGCATTTTTCTCCCACACAATAAAAGCTCAGGAGGCCAATATG
GGCTTGTTGGATGAGATTCTAAAACAGGAAATTCGCCTTATTGATTATGAGAAAATGGTG
GATCATAGAGGAGTACGGGTAGTGGCATTTGGACAGTGGGCTGGTGTGGCAGGAATGATC
AACATTTTACATGGAATGGGTTTAAGGCTCCTTGCTTTGGGACATCACACACCTTTTATG
CACATTGGCATGGCTCATAACTACAGGAATAGCAGTCAGGCTGTGCAAGCTGTCCGTGAT
GCTGGCTATGAAATATCTTTGGGTTTGATGCCTAAGTCAATAGGACCCTTAACATTTGTG
TTCACAGGAACTGGTAATGTTTCTAAGGGAGCCCAAGCAATCTTTAATGAGCTACCTTGT
GAATATGTGGAGCCCCATGAATTAAAAGAAGTTTCCCAAACTGGAGACCTCAGAAAAGTG
TATGGGACGGTGTTAAGTCGTCATCATCATCTTGTCAGGAAAACAGATGCTGTGTATGAT
CCTGCAGAGTATGACAAACATCCGGAGCGCTACATAAGTCGTTTTAATACTGATATTGCA
CCCTATACAACTTGCTTAATTAATGGAATCTACTGGGAACAAAACACTCCTCGCCTCCTA
ACCCGCCAAGATGCTCAGAGTCTCCTGGCTCCGGGCAAGTTCTCACCTGCTGGTGTGGAA
GGCTGCCCTGCATTACCACACAAACTCGTGGCAATATGTGACATTTCAGCTGACACAGGA
GGGTCTATAGAGTTTATGACTGAGTGTACAACAATAGAGCATCCCTTTTGCATGTATGAT
GCAGACCAGCATATTATTCATGACAGTGTTGAAGGCTCGGGGATCCTGATGTGTTCCATT
GACAATTTGCCGGCACAGCTCCCAATTGAAGCTACAGAATGCTTTGGAGACATGCTTTAC
CCTTATGTTGAAGAAATGATATTATCAGACGCGACACAGCCTCTTGAAAGTCAGAATTTT
TCTCCTGTGGTGAGAGATGCAGTGATTACATCCAACGGTACATTACCTGATAAATATAAA
TATATCCAGACACTCCGGGAGAGCAGGGAACGTGCTCAGTCACTTTCAATGGGCACCAGG
AGAAAGGTTTTGGTTCTTGGATCTGGCTACATATCTGAGCCTGTATTAGAATATTTATCA
AGAGATGGCAATATAGAAATAACAGTAGGATCTGACATGAAGAATCAAATTGAACAGTTA
GGCAAGAAATATAATATTAATCCTGTTAGCATGGACATTTGTAAACAAGAAGAGAAGCTG
GGCTTCTTGGTGGCAAAACAGGATCTTGTCATCAGCTTGTTGCCTTATGTATTGCACCCT
CTTGTGGCCAAGGCCTGCATCACAAACAAAGTTAACATGGTCACTGCAAGCTACATCACA
CCAGCACTAAAAGAATTGGAAAAGAGTGTGGAAGATGCTGGCATCACAATCATTGGTGAA
TTGGGATTGGACCCTGGTCTGGATCACATGTTAGCAATGGAAACAATAGATAAAGCCAAG
GAAGTGGGAGCCACGATTGAATCATATATTTCCTACTGTGGTGGGCTTCCAGCCCCTGAA
CATTCAAACAATCCATTGAGATATAAATTTAGCTGGAGTCCAGTGGGAGTTTTGATGAAT
GTAATGCAGTCTGCCACCTATCTGCTCGATGGAAAGGTTGTGAATGTTGCAGGAGGCATC
TCCTTTCTTGATGCCGTTACGTCCATGGATTTTTTTCCAGGATTAAATTTGGAAGGCTAT
CCTAACAGAGACAGTACGAAATATGCTGAGATTTATGGCATTTCTTCTGCTCACACTTTG
TTGCGGGGGACACTGAGATATAAGGGATATATGAAAGCTTTGAATGGATTTGTAAAATTA
GGTCTTATAAACAGAGAAGCGCTTCCTGCCTTTAGACCTGAGGCCAACCCTCTCACCTGG
AAACAACTCCTCTGTGACCTAGTTGGGATTTCACCCTCCTCTGAGCATGATGTGTTGAAG
GAAGCTGTTCTTAAGAAACTAGGAGGAGACAATACCCAGTTGGAGGCTGCTGAATGGTTG
GGCTTACTTGGGGATGAACAAGTTCCTCAGGCAGAGTCCATTCTGGATGCCCTCTCCAAG
CATTTGGTCATGAAGCTTTCCTATGGTCCTGAAGAAAAAGATATGATTGTGATGAGAGAC
AGCTTTGGAATCAGACATCCTTCTGGACATTTAGAACATAAAACGATTGATCTTGTGGCT
TATGGGGACATCAATGGCTTTTCAGCCATGGCTAAAACCGTGGGGTTACCCACCGCCATG
GCAGCCAAAATGTTGCTTGATGGTGAAATTGGAGCCAAAGGCCTAATGGGGCCCTTTTCA
AAGGAGATCTATGGACCAATATTGGAGCGAATTAAAGCAGAAGGCATTATATATACTACA
CAGAGTACAATTAAACCATAA
Enzyme 1 GenBank Gene ID AF229180 Link Image
Enzyme 1 GeneCard ID AASS Link Image
Enzyme 1 GenAtlas ID AASS Link Image
Enzyme 1 HGNC ID HGNC:17366 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q31.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Sacksteder KA, Biery BJ, Morrell JC, Goodman BK, Geisbrecht BV, Cox RP, Gould SJ, Geraghty MT: Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. Am J Hum Genet. 2000 Jun;66(6):1736-43. Epub 2000 Apr 20. [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. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13066
Enzyme 2 Name Acyl-CoA synthetase family member 4
Enzyme 2 Synonyms
  1. Protein NRPS998
Enzyme 2 Gene Name AASDH
Enzyme 2 Protein Sequence >Acyl-CoA synthetase family member 4 
MTLQELVHKAASCYMDRVAVCFDECNNQLPVYYTYKTVVNAASELSNFLLLHCDFQGIRE
IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKFK
SFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNLMLNDGKEKYEKEKIKSISSEHVNEEKA
EEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL
TFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQL
IKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPE
KTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL
GTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE
KLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY
INLKSENKLSGKEDLWEKLQYLWKSTLNLPEDLLRVPDESLFLNSGGDSLKSIRLLSEIE
KLVGTSVPGLLEIILSSSILEIYNHILQTVVPDEDVTFRKSCATKRKLSDINQEEASGTS
LHQKAIMTFTCHNEINAFVVLSRGSQILSLNSTRFLTKLGHCSSACPSDSVSQTNIQNLK
GLNSPVLIGKSKDPSCVAKVSEEGKPAIGTQKMELHVRWRSDTGKCVDASPLVVIPTFDK
SSTTVYIGSHSHRMKAVDFYSGKVKWEQILGDRIESSACVSKCGNFIVVGCYNGLVYVLK
SNSGEKYWMFTTEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFS
SPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNL
LCFTHFGEQVWQFSTSGPIFSSPCTSPSEQKIFFGSHDCFIYCCNMKGHLQWKFETTSRV
YATPFAFHNYNGSNEMLLAAASTDGKVWILESQSGQLQSVYELPGEVFSSPVVLESMLII
GCRDNYVYCLDLLGGNQK
Enzyme 2 Number of Residues 1098
Enzyme 2 Molecular Weight 122596.1
Enzyme 2 Theoretical pI 7.26
Enzyme 2 GO Classification
Function
  • acyl carrier activity
  • binding
  • catalytic activity
  • cofactor binding
  • substrate-specific transporter activity
  • transporter activity
Process
  • metabolic process
Component
—
Enzyme 2 General Function Involved in acyl carrier activity
Enzyme 2 Specific Function Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 45580730 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q4L235 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ACSF4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3297 bp 
ATGACTCTTCAGGAATTGGTGCATAAGGCTGCCTCCTGTTATATGGACAGAGTAGCTGTA
TGTTTTGATGAATGCAACAACCAGCTTCCAGTTTACTACACCTACAAGACTGTGGTTAAT
GCTGCTTCTGAATTATCAAATTTTCTGCTGTTACACTGTGACTTTCAAGGAATTCGGGAA
ATTGGTCTCTACTGCCAACCTGGGATAGACTTACCCTCTTGGATTTTAGGAATTCTCCAA
GTCCCGGCTGCTTATGTACCTATCGAGCCAGATTCACCACCGTCATTATCAACTCATTTT
ATGAAAAAATGTAATCTAAAGTATATCCTTGTTGAAAAAAAACAAATTAATAAATTTAAA
TCTTTTCATGAAACATTATTGAACTATGATACATTTACAGTGGAACATAATGACCTAGTG
CTCTTCAGACTTCACTGGAAAAATACTGAGGTGAACTTGATGCTAAATGATGGAAAAGAG
AAATATGAAAAAGAAAAAATAAAAAGCATAAGTTCTGAGCATGTCAATGAAGAAAAAGCA
GAAGAACACATGGATCTGAGGCTAAAGCATTGCTTAGCCTATGTTCTACATACATCAGGG
ACTACAGGGATACCGAAGATTGTCAGAGTGCCTCATAAGTGTATAGTACCAAATATCCAG
CATTTTCGGGTACTTTTTGACATCACACAAGAAGATGTTTTGTTTCTGGCTTCACCTCTG
ACCTTCGATCCTTCTGTTGTGGAAATATTTCTTGCTCTATCAAGTGGTGCCTCTCTGCTT
ATTGTACCAACTTCCGTCAAGTTGCTCCCATCAAAATTAGCCAGCGTTCTCTTTTCCCAT
CATAGAGTGACTGTTTTGCAGGCAACACCAACATTGCTTAGAAGATTTGGATCTCAGCTT
ATCAAGTCAACTGTTTTGTCAGCCACTACTTCTCTTCGAGTATTAGCCCTTGGTGGTGAA
GCGTTTCCATCATTGACAGTTCTCAGAAGCTGGAGAGGAGAAGGCAATAAAACACAAATA
TTTAATGTTTATGGTATCACAGAGGTATCAAGTTGGGCGACCATTTATAGGATTCCAGAG
AAGACTCTTAACTCTACTCTCAAATGTGAATTGCCTGTACAACTGGGATTTCCACTTCTT
GGAACAGTAGTTGAAGTCAGAGATACTAATGGCTTCACAATTCAGGAAGGCAGTGGCCAA
GTATTTTTAGGTGGCAGAAACAGAGTGTGTTTTCTTGATGATGAAGTGACAGTACCACTT
GGCACAATGCGAGCTACAGGAGACTTTGTGACTGTGAAAGATGGAGAGATTTTTTTTTTG
GGACGAAAAGACAGTCAGATCAAACGTCATGGCAAACGTCTTAACATTGAACTTGTGCAA
CAGGTTGCTGAAGAGCTTCAGCAAGTGGAGTCTTGTGCAGTTACATGGTATAATCAGGAA
AAATTAATTCTCTTCATGGTGTCTAAAGATGCTTCAGTAAAAGAATACATCTTTAAAGAA
CTGCAGAAATATCTTCCAAGTCATGCAGTCCCGGATGAGCTTGTATTGATCGACTCTCTA
CCATTTACATCCCACGGCAAAATTGATGTTTCTGAGTTAAACAAGATATATTTAAACTAC
ATAAACTTGAAGTCTGAGAATAAGCTCAGTGGGAAAGAGGACCTTTGGGAAAAATTACAG
TATTTGTGGAAGTCTACTCTGAATCTCCCAGAAGATCTTTTGAGGGTTCCTGATGAGTCA
CTCTTCTTAAATAGTGGTGGAGATTCCTTAAAGTCCATCCGGCTCCTCAGTGAGATTGAA
AAACTTGTTGGTACATCAGTACCTGGGCTTCTGGAAATTATTCTCAGCAGTTCCATTTTA
GAGATTTATAATCACATCCTTCAAACAGTGGTTCCAGATGAAGATGTGACATTCAGGAAG
AGTTGTGCCACAAAAAGGAAACTCAGCGACATTAATCAAGAGGAAGCCAGTGGAACATCT
TTACATCAGAAAGCCATCATGACTTTCACTTGCCACAATGAGATTAATGCTTTTGTTGTA
CTGAGCAGAGGGAGTCAAATTTTGTCTCTGAATTCCACTAGGTTTTTAACAAAGTTAGGA
CATTGCTCTTCAGCCTGTCCTTCTGACTCAGTTTCACAGACCAACATTCAAAATTTGAAA
GGCTTAAATTCTCCAGTTCTTATTGGGAAGTCAAAAGATCCATCCTGTGTTGCAAAAGTT
TCTGAAGAGGGGAAACCTGCGATAGGGACTCAGAAAATGGAGTTACATGTGAGGTGGAGG
TCAGACACAGGCAAATGTGTAGATGCTTCACCGCTGGTTGTAATACCCACTTTTGATAAG
TCATCTACAACTGTGTACATTGGTTCCCATTCTCATAGAATGAAGGCAGTTGACTTTTAC
TCTGGGAAGGTAAAATGGGAACAGATTTTGGGAGATCGAATTGAATCCTCAGCATGTGTA
TCTAAGTGTGGAAACTTTATTGTGGTGGGCTGTTATAATGGATTAGTTTATGTTCTGAAA
AGTAATAGTGGAGAAAAATACTGGATGTTTACTACTGAAGATGCTGTCAAAAGCTCGGCA
ACCATGGATCCAACCACAGGACTCATTTACATTGGATCTCATGACCAGCACGCATATGCT
TTAGATATTTATAGAAAGAAGTGTGTTTGGAAGTCAAAATGTGGAGGAACTGTCTTTTCC
TCTCCGTGTTTGAACCTGATTCCACATCATTTGTATTTTGCTACATTGGGAGGACTTTTA
CTGGCTGTAAATCCTGCTACTGGGAACGTTATTTGGAAACATTCCTGTGGAAAACCACTC
TTCTCTTCCCCACAATGTTGCTCACAGTATATTTGTATTGGCTGTGTAGATGGGAATTTA
CTCTGCTTTACTCACTTTGGAGAACAGGTTTGGCAGTTCTCTACCAGTGGACCAATCTTT
TCATCCCCGTGTACCTCACCATCAGAGCAAAAAATATTTTTTGGTTCCCATGATTGCTTT
ATCTACTGTTGTAACATGAAAGGTCACCTGCAGTGGAAATTTGAAACTACTTCAAGGGTC
TATGCAACACCGTTTGCTTTCCATAACTACAATGGCAGCAATGAAATGTTGCTGGCAGCA
GCATCTACTGATGGGAAAGTGTGGATCTTGGAATCTCAGAGTGGACAATTGCAAAGTGTT
TATGAACTTCCTGGAGAAGTCTTCTCTTCTCCTGTGGTCCTGGAATCAATGCTCATTATT
GGGTGTAGAGATAATTATGTTTATTGTCTGGATTTATTGGGTGGCAATCAAAAATAA
Enzyme 2 GenBank Gene ID NM_181806.2 Link Image
Enzyme 2 GeneCard ID AASDH Link Image
Enzyme 2 GenAtlas ID AASDH Link Image
Enzyme 2 HGNC ID HGNC:23993 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Wang L, Jil C, Xu Y, Xu J, Dai J, Wu Q, Wu M, Zou X, Sun L, Gu S, Xie Y, Mao Y: Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase. Mol Biol Rep. 2005 Mar;32(1):47-53. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
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Enzyme 2 Metabolite References Not Available