AMY2A

Amylase, alpha 2A (pancreatic)

PDB rendering based on 1b2y.

Available structures

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

Identifiers

AMY2A ; AMY2; AMY2B; PA

External IDs

OMIM: 104650 MGI: 88019 HomoloGene: 20179 IUPHAR: 2596 ChEMBL: 2045 GeneCards: AMY2A Gene

Gene ontology
Molecular function	• alpha-amylase activity • calcium ion binding • chloride ion binding
Cellular component	• extracellular region • extracellular space • extracellular vesicular exosome
Biological process	• carbohydrate metabolic process • carbohydrate catabolic process • polysaccharide digestion • small molecule metabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

ENSG00000243480

ENSMUSG00000074264

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
104.16 – 104.17 Mb

Chr 3:
113.56 – 113.61 Mb

PubMed search

Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene.^[1]^[2]

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.^[2]

References

↑ 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.
↑ 2.0 2.1 "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic".

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". Gene 60 (1): 57–64. doi:10.1016/0378-1119(87)90213-7. PMID 2450054.
Gumucio DL, Wiebauer K, Caldwell RM et al. (1988). "Concerted evolution of human amylase genes". Mol. Cell. Biol. 8 (3): 1197–205. 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.
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.

PDB gallery

1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE

1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN

1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE

1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT

1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes

1jxj: Role of mobile loop in the mechanism of human salivary amylase

1jxk: Role of the mobile loop in the mechanism of human salivary amylase

1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase

1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids

1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids

1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE

1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE

1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase

1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant

1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme

1nm9: Crystal structure of recombinant human salivary amylase mutant W58A

1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity

1smd: HUMAN SALIVARY AMYLASE

1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam

1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam

1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors

1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts

1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts

1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts

1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts

1xgz: Structure of the N298S variant of human pancreatic alpha-amylase

1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose

1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride

1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose

1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer

1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues

2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT

3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT