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AMY1A





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Alpha-amylase1 is an enzyme that in humans is encoded by the AMY1A gene.[3] This gene is found in many organisms.

AMY1A
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesAMY1A, AMY1, amylase, alpha 1A (salivary), amylase alpha 1A (salivary), amylase alpha 1A
External IDsOMIM: 104700; HomoloGene: 133998; GeneCards: AMY1A; OMA:AMY1A - orthologs
EC number3.2.1.1
Orthologs
SpeciesHumanMouse
Entrez

276

n/a

Ensembl

ENSG00000237763

n/a

UniProt

P04745

n/a

RefSeq (mRNA)

NM_004038
NM_001008221

n/a

RefSeq (protein)

NP_001008220
NP_001333709
NP_001008222
NP_004029
NP_001008219

n/a

Location (UCSC)Chr 1: 103.66 – 103.66 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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.[3]

See also

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References

edit
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000237763 – Ensembl, May 2017
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ a b "Entrez Gene: AMY1A amylase, alpha 1A; salivary".
    • edit

    Further reading

    edit
  • 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. hdl:11094/36665. PMID 2450054.
  • 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.
  • 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. S2CID 37322144.
  • 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. 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.
  • 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. S2CID 6897149.
  • 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. Bibcode:2002PNAS...9916899M. 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. S2CID 83561963.


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    Last edited on 20 October 2022, at 10:28  





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