AMY2A

AMY2A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1B2Y, 1BSI, 1CPU, 1HNY, 1KB3, 1KBB, 1KBK, 1KGU, 1KGW, 1KGX, 1U2Y, 1U30, 1U33, 1XCW, 1XCX, 1XD0, 1XD1, 1XGZ, 1XH0, 1XH1, 1XH2, 2CPU, 2QMK, 2QV4, 3BAI, 3BAJ, 3BAK, 3BAW, 3BAX, 3BAY, 3CPU, 3IJ7, 3IJ8, 3IJ9, 3OLD, 3OLE, 3OLG, 3OLI, 4GQQ, 4GQR, 4W93, 4X9Y, 5EMY
Identifiers
Aliases	AMY2A , AMY2, AMY2B, PA, amylase, alpha 2A (pancreatic), amylase alpha 2A (pancreatic), amylase alpha 2A
External IDs	OMIM: 104650; MGI: 88019; HomoloGene: 20179; GeneCards: AMY2A; OMA:AMY2A - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p21.1 Start 103,617,427 bp [1] End 103,625,780 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3 F3|3 49.35 cM Start 113,349,359 bp [2] End 113,400,348 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans duodenum testicle nucleus accumbens fundus ectocervix putamen caudate nucleus right lobe of liver Top expressed in parotid gland lacrimal gland submandibular gland intercostal muscle left lobe of liver white adipose tissue neural layer of retina tunica adventitia of aorta subcutaneous adipose tissue lactiferous gland More reference expression data BioGPS n/a
Gene ontology Molecular function chloride ion binding calcium ion binding catalytic activity alpha-amylase activity hydrolase activity metal ion binding hydrolase activity, acting on glycosyl bonds cation binding Cellular component extracellular region extracellular exosome extracellular space Biological process carbohydrate catabolic process polysaccharide digestion metabolism carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 279 11722 Ensembl ENSG00000243480 ENSMUSG00000074264 UniProt P04746 P00687 RefSeq (mRNA) NM_000699 NM_001110505 NM_007446 RefSeq (protein) NP_000690 NP_001103975 NP_031472 Location (UCSC) Chr 1: 103.62 – 103.63 Mb Chr 3: 113.35 – 113.4 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene. ^{[5] [6]}

Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000243480 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000074264 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR (Jul 1988). "Human pancreatic amylase is encoded by two different genes". Nucleic Acids Res. 16 (10): 4724. doi:10.1093/nar/16.10.4724. PMC   336663 . PMID   3260028.
6. "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic".

External links

• Human AMY2A genome location and AMY2A gene details page in the UCSC Genome Browser .

See also

• AMY1A

Further reading

• Kaczmarek MJ, Rosenmund H (1977). "The action of human pancreatic and salivary isoamylases on starch and glycogen". Clin. Chim. Acta. 79 (1): 69–73. doi:10.1016/0009-8981(77)90462-4. PMID   890964.
• Jacob M, Lainé J, LeBel D (1993). "Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP-2) bind to immobilized or polymerized amylase". Biochem. Cell Biol. 70 (10–11): 1105–14. doi:10.1139/o92-156. PMID   1284286.
• Groot PC, Mager WH, Henriquez NV, et al. (1991). "Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers". Genomics. 8 (1): 97–105. doi:10.1016/0888-7543(90)90230-R. PMID   2081604.
• Nishide T, Nakamura Y, Emi M, et al. (1986). "Primary structure of human salivary alpha-amylase gene". Gene. 41 (2–3): 299–304. doi:10.1016/0378-1119(86)90110-1. PMID   2423416.
• Horii A, Emi M, Tomita N, et al. (1988). "Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene" (PDF). Gene. 60 (1): 57–64. doi:10.1016/0378-1119(87)90213-7. hdl: 11094/36665 . PMID   2450054. S2CID   85098215.
• Gumucio DL, Wiebauer K, Caldwell RM, et al. (1988). "Concerted evolution of human amylase genes". Mol. Cell. Biol. 8 (3): 1197–205. doi:10.1128/mcb.8.3.1197. PMC   363264 . PMID   2452973.
• Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH (1988). "Expression of the human amylase genes: recent origin of a salivary amylase promoter from an actin pseudogene". Nucleic Acids Res. 16 (17): 8261–76. doi:10.1093/nar/16.17.8261. PMC   338557 . PMID   2458567.
• Groot PC, Bleeker MJ, Pronk JC, et al. (1989). "The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes". Genomics. 5 (1): 29–42. doi:10.1016/0888-7543(89)90083-9. PMID   2788608.
• Wise RJ, Karn RC, Larsen SH, et al. (1986). "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. 2 (5): 307–22. PMID   6336237.
• Tricoli JV, Shows TB (1984). "Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1". Somat. Cell Mol. Genet. 10 (2): 205–10. doi:10.1007/BF01534909. PMID   6608795. S2CID   21230969.
• Nishide T, Emi M, Nakamura Y, Matsubara K (1984). "Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected]". Gene. 28 (2): 263–70. doi:10.1016/0378-1119(84)90265-8. PMID   6610603.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Qian M, Haser R, Buisson G, et al. (1994). "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. 33 (20): 6284–94. doi:10.1021/bi00186a031. PMID   8193143.
• Brayer GD, Luo Y, Withers SG (1996). "The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes". Protein Sci. 4 (9): 1730–42. doi:10.1002/pro.5560040908. PMC   2143216 . PMID   8528071.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Rydberg EH, Sidhu G, Vo HC, et al. (1999). "Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris". Protein Sci. 8 (3): 635–43. doi:10.1110/ps.8.3.635. PMC   2144294 . PMID   10091666.
• Brayer GD, Sidhu G, Maurus R, et al. (2000). "Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques". Biochemistry. 39 (16): 4778–91. doi:10.1021/bi9921182. PMID   10769135.
• Aughsteen AA (2001). "A comparative immunohistochemical study on amylase localization in the rat and human exocrine pancreas". Saudi Medical Journal. 22 (5): 410–5. PMID   11376382.
• Numao S, Maurus R, Sidhu G, et al. (2002). "Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase". Biochemistry. 41 (1): 215–25. doi:10.1021/bi0115636. PMID   11772019.