AMY1A

Amylase, alpha 1A (salivary)

PDB rendering based on 1b2y.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1C8Q, 1JXJ, 1JXK, 1MFU, 1MFV, 1NM9, 1Q4N, 1SMD, 1XV8, 1Z32, 3BLK, 3BLP, 3DHP

Identifiers

Symbols

AMY1A ; AMY1

External IDs

OMIM: 104700 MGI: 88020 HomoloGene: 133998 ChEMBL: 2478 GeneCards: AMY1A Gene

EC number

3.2.1.1

Gene ontology
Molecular function	• catalytic activity • alpha-amylase activity • calcium ion binding • protein binding • hydrolase activity, acting on glycosyl bonds • chloride ion binding • cation binding
Cellular component	• extracellular space
Biological process	• carbohydrate metabolic process • digestion • metabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
104.2 – 104.21 Mb

Chr 3:
113.56 – 113.61 Mb

PubMed search

Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene.^[1] This gene is found in many organisms, see Alpha-Amylase.

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 salivary gland. Alternative splicing results in multiple transcript variants encoding the same protein.^[1]

References

↑ 1.0 1.1 "Entrez Gene: AMY1A amylase, alpha 1A; salivary".

Bank RA, Hettema EH, Arwert F et al. (1991). "Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase.". Electrophoresis 12 (1): 74–9. doi:10.1002/elps.1150120114. PMID 1710976.
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.
Davis MM, Hodes ME, Munsick RA et al. (1986). "Pancreatic amylase expression in human pancreatic development". Hybridoma 5 (2): 137–45. doi:10.1089/hyb.1986.5.137. PMID 2424823.
Handy DE, Larsen SH, Karn RC, Hodes ME (1987). "Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1". Mol. Biol. Med. 4 (3): 145–55. PMID 2442579.
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.
Pronk JC, Frants RR, Jansen W et al. (1982). "Evidence of duplication of the human salivary amylase gene". Hum. Genet. 60 (1): 32–5. doi:10.1007/BF00281260. PMID 6176528.
Zabel BU, Naylor SL, Sakaguchi AY et al. (1984). "High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization". Proc. Natl. Acad. Sci. U.S.A. 80 (22): 6932–6. doi:10.1073/pnas.80.22.6932. PMC 390100. PMID 6196780.
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.
Seyama K, Nukiwa T, Takahashi K et al. (1994). "Amylase mRNA transcripts in normal tissues and neoplasms: the implication of different expressions of amylase isogenes". J. Cancer Res. Clin. Oncol. 120 (4): 213–20. doi:10.1007/BF01372559. PMID 7507116.
Ragunath C, Sundar K, Ramasubbu N (2002). "Expression, characterization, and biochemical properties of recombinant human salivary amylase". Protein Expr. Purif. 24 (2): 202–11. doi:10.1006/prep.2001.1559. PMID 11858714.
Hokari S, Miura K, Koyama I et al. (2002). "A restriction endonuclease assay for expression of human alpha-amylase isozymes". Clin. Chim. Acta 322 (1–2): 113–6. doi:10.1016/S0009-8981(02)00161-4. PMID 12104089.
Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (2003). "AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex". J. Biol. Chem. 277 (52): 50885–92. doi:10.1074/jbc.M206387200. PMID 12414807.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ramasubbu N, Ragunath C, Mishra PJ (2003). "Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase". J. Mol. Biol. 325 (5): 1061–76. doi:10.1016/S0022-2836(02)01326-8. PMID 12527308.
Kandra L, Gyémánt G, Remenyik J et al. (2003). "Subsite mapping of human salivary alpha-amylase and the mutant Y151M". FEBS Lett. 544 (1–3): 194–8. doi:10.1016/S0014-5793(03)00495-2. PMID 12782315.

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

AMY1A

References

Further reading