AMY2A

AMY2A

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, 4W93, 4X9Y, 5EMY

Identifiers

AMY2A, AMY2, AMY2B, PA, amylase, alpha 2A (pancreatic)

External IDs

MGI: 88019 HomoloGene: 20179 GeneCards: AMY2A

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 space • extracellular region • extracellular exosome
Biological process	• carbohydrate catabolic process • polysaccharide digestion • metabolic process • carbohydrate metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse


279


11722


ENSG00000243480


ENSMUSG00000074264


P04746


P04745 P00687

RefSeq (mRNA)


NM_000699


NM_001110505 NM_007446

RefSeq (protein)


NP_000690.1

NP_001008219.1 NP_001008220.1 NP_001008222.1 NP_004029.2 NP_001103975.1
NP_031472.2

Location (UCSC)

Chr 1: 103.62 – 103.63 Mb

Chr 3: 113.56 – 113.61 Mb

PubMed search

^[1]

^[2]

View/Edit Human

View/Edit Mouse

Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene.^[3]^[4]

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.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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".

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

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