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Showing Protein Pancreatic alpha-amylase (HMDBP02084)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP02084
Secondary Accession Numbers
  • 7565
  • HMDBP07155
Name Pancreatic alpha-amylase
Synonyms
  1. 1,4-alpha-D-glucan glucanohydrolase
  2. PA
Gene Name AMY2A
Protein Type Unknown
Biological Properties
General Function Involved in catalytic activity
Specific Function Not Available
Pathways
  • Carbohydrate digestion and absorption
  • Pancreatic secretion
  • Starch and sucrose metabolism
Reactions
Starch + Water → Dextrin + Starch details
GO Classification
Biological Process
small molecule metabolic process
carbohydrate catabolic process
polysaccharide digestion
Cellular Component
extracellular space
Function
ion binding
cation binding
binding
catalytic activity
Molecular Function
alpha-amylase activity
chloride ion binding
calcium ion binding
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
Cellular Location
  1. Secreted
  2. extracellular space
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs AMY2A
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
Protein Properties
Number of Residues 511
Molecular Weight Not Available
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Pancreatic alpha-amylase
MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGL
LDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
GenBank ID Protein 529397
UniProtKB/Swiss-Prot ID P04746
UniProtKB/Swiss-Prot Entry Name AMYP_HUMAN
PDB IDs
GenBank Gene ID M28443
GeneCard ID AMY2A
GenAtlas ID AMY2A
HGNC ID HGNC:477
References
General References
  1. 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:15489334 ]
  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:6610603 ]
  3. 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:2452973 ]
  4. 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:2450054 ]
  5. 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:6336237 ]
  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:3260028 ]
  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:8193143 ]
  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:8528071 ]
  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:10091666 ]
  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:10769135 ]
  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:11772019 ]
  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:11914097 ]