AMY2A

AMY2A
Identifiers
Aliases	AMY2A, AMY2, AMY2B, PA, amylase, alpha 2A (pancreatic), amylase alpha 2A (pancreatic), amylase alpha 2A
External IDs	OMIM: 104650; MGI: 88019; GeneCards: 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
Enzyme activity
Gene location (Human)
Chr.	Chromosome 1 (human)
End	103,625,780 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	113,400,348 bp
RNA expression pattern
	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
	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
Databases	NCBI: entry; OMA: entry
	279
	11722
	ENSG00000243480
	ENSMUSG00000074264
	P04746
	P00687
	NM_000699
	NM_001110505; NM_007446
	NP_000690
	NP_001103975; NP_031472
	Wikidata
View/Edit Human	View/Edit Mouse

Alpha-amylase 2A is a digestive enzyme that in humans is encoded by the AMY2A gene.^[5]^[6] This enzyme functions to break down carbohydrates and especially starch.^[7] The enzymes AMY2A and AMY2B (sometimes collectively called AMY2) are the primary alpha-amylases secreted by the acinar cells of the pancreas into pancreatic juice, which is released into the duodenum (the first segment of the small intestines).^[7]^[8]

Function

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 (AMY1A, AMY1B, AMY1C)^[7] or pancreas (AMY2A, AMY2B)^[7]. This gene encodes an amylase isoenzyme produced by the pancreas.^[6] Like the saliva AMY1 enzymes, the number of AMY2-encoding genes varies from individual to individual,^[7] however the AMY2A and AMY2B proteins are ~99% similar but not identical.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000243480 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000074264 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic".
1 2 3 4 5 Butterworth PJ, Warren FJ, Ellis PR (July 2011). "Human α‐amylase and starch digestion: An interesting marriage". Starch‐Stärke. 63 (7): 395–405. doi:10.1002/star.201000150.
1 2 "Pancreatic alpha-amylase". uniprot.org. UniProt consortium. Retrieved 2026-09-21.

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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.
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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.
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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.