AMY1A

AMY1A

Amylase, alpha 1A; salivary, also known as AMY1A, is a human gene.cite web | title = Entrez Gene: AMY1A amylase, alpha 1A; salivary| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=276| accessdate = ] This gene is found in many organisms, see Alpha-Amylase.

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: AMY1A amylase, alpha 1A; salivary| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=276| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Bank RA, Hettema EH, Arwert F, "et al." |title=Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. |journal=Electrophoresis |volume=12 |issue= 1 |pages= 74–9 |year= 1991 |pmid= 1710976 |doi= 10.1002/elps.1150120114
*cite journal | author=Groot PC, Mager WH, Henriquez NV, "et al." |title=Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers. |journal=Genomics |volume=8 |issue= 1 |pages= 97–105 |year= 1991 |pmid= 2081604 |doi=
*cite journal | author=Nishide T, Nakamura Y, Emi M, "et al." |title=Primary structure of human salivary alpha-amylase gene. |journal=Gene |volume=41 |issue= 2-3 |pages= 299–304 |year= 1986 |pmid= 2423416 |doi=
*cite journal | author=Davis MM, Hodes ME, Munsick RA, "et al." |title=Pancreatic amylase expression in human pancreatic development. |journal=Hybridoma |volume=5 |issue= 2 |pages= 137–45 |year= 1986 |pmid= 2424823 |doi=
*cite journal | author=Handy DE, Larsen SH, Karn RC, Hodes ME |title=Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1. |journal=Mol. Biol. Med. |volume=4 |issue= 3 |pages= 145–55 |year= 1987 |pmid= 2442579 |doi=
*cite journal | author=Horii A, Emi M, Tomita N, "et al." |title=Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene. |journal=Gene |volume=60 |issue= 1 |pages= 57–64 |year= 1988 |pmid= 2450054 |doi=
*cite journal | author=Gumucio DL, Wiebauer K, Caldwell RM, "et al." |title=Concerted evolution of human amylase genes. |journal=Mol. Cell. Biol. |volume=8 |issue= 3 |pages= 1197–205 |year= 1988 |pmid= 2452973 |doi=
*cite journal | author=Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH |title=Expression of the human amylase genes: recent origin of a salivary amylase promoter from an actin pseudogene. |journal=Nucleic Acids Res. |volume=16 |issue= 17 |pages= 8261–76 |year= 1988 |pmid= 2458567 |doi=
*cite journal | author=Groot PC, Bleeker MJ, Pronk JC, "et al." |title=The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes. |journal=Genomics |volume=5 |issue= 1 |pages= 29–42 |year= 1989 |pmid= 2788608 |doi=
*cite journal | author=Pronk JC, Frants RR, Jansen W, "et al." |title=Evidence of duplication of the human salivary amylase gene. |journal=Hum. Genet. |volume=60 |issue= 1 |pages= 32–5 |year= 1982 |pmid= 6176528 |doi=
*cite journal | author=Zabel BU, Naylor SL, Sakaguchi AY, "et al." |title=High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 22 |pages= 6932–6 |year= 1984 |pmid= 6196780 |doi=
*cite journal | author=Tricoli JV, Shows TB |title=Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 2 |pages= 205–10 |year= 1984 |pmid= 6608795 |doi=
*cite journal | author=Nishide T, Emi M, Nakamura Y, Matsubara K |title=Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] |journal=Gene |volume=28 |issue= 2 |pages= 263–70 |year= 1984 |pmid= 6610603 |doi=
*cite journal | author=Seyama K, Nukiwa T, Takahashi K, "et al." |title=Amylase mRNA transcripts in normal tissues and neoplasms: the implication of different expressions of amylase isogenes. |journal=J. Cancer Res. Clin. Oncol. |volume=120 |issue= 4 |pages= 213–20 |year= 1994 |pmid= 7507116 |doi=
*cite journal | author=Ragunath C, Sundar K, Ramasubbu N |title=Expression, characterization, and biochemical properties of recombinant human salivary amylase. |journal=Protein Expr. Purif. |volume=24 |issue= 2 |pages= 202–11 |year= 2002 |pmid= 11858714 |doi= 10.1006/prep.2001.1559
*cite journal | author=Hokari S, Miura K, Koyama I, "et al." |title=A restriction endonuclease assay for expression of human alpha-amylase isozymes. |journal=Clin. Chim. Acta |volume=322 |issue= 1-2 |pages= 113–6 |year= 2002 |pmid= 12104089 |doi=
*cite journal | author=Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50885–92 |year= 2003 |pmid= 12414807 |doi= 10.1074/jbc.M206387200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ramasubbu N, Ragunath C, Mishra PJ |title=Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. |journal=J. Mol. Biol. |volume=325 |issue= 5 |pages= 1061–76 |year= 2003 |pmid= 12527308 |doi=
*cite journal | author=Kandra L, Gyémánt G, Remenyik J, "et al." |title=Subsite mapping of human salivary alpha-amylase and the mutant Y151M. |journal=FEBS Lett. |volume=544 |issue= 1-3 |pages= 194–8 |year= 2003 |pmid= 12782315 |doi=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать реферат

Look at other dictionaries:

  • Alpha-Amylase — α Amylase is the major form of amylase found in humans and other mammals.Amylase in human physiologyAlthough found in many tissues, amylase is most prominent in pancreatic juice and saliva which each have their own isoform of human α amylase.… …   Wikipedia

  • Speichel-Amylase — Bändermodell nach PDB  …   Deutsch Wikipedia

  • α-amylase — L α amylase pancréatique (l ion Ca++ est représenté par le rond jaune pâle en bas au centre) Caractéristiques générales Nom approuvé 4 α D glucane glucanohydrolase …   Wikipédia en Français

  • Alpha-Amylase — Amylasen sind Enzyme, die bei den meisten Lebewesen vorkommen, und die Polysaccharide abbauen. Heutzutage wird α Amylase auch gentechnisch hergestellt. [1] Ihre Wirkung besteht darin, dass sie Polysaccharide (z. B. Stärke) an den… …   Deutsch Wikipedia

  • Amylase — Amylasen sind Enzyme, die bei den meisten Lebewesen vorkommen, und die Polysaccharide abbauen. Heutzutage wird α Amylase auch gentechnisch hergestellt. [1] Ihre Wirkung besteht darin, dass sie Polysaccharide (z. B. Stärke) an den… …   Deutsch Wikipedia

  • Amylasen — (von griechisch Amylon = Stärkemehl) sind Enzyme, die bei den meisten Lebewesen vorkommen und dort Polysaccharide abbauen. Heutzutage wird α Amylase auch gentechnisch hergestellt. [1] Ihre Wirkung besteht darin, dass sie Polysaccharide (z. B.… …   Deutsch Wikipedia

  • Diastase (Enzym) — Amylasen sind Enzyme, die bei den meisten Lebewesen vorkommen, und die Polysaccharide abbauen. Heutzutage wird α Amylase auch gentechnisch hergestellt. [1] Ihre Wirkung besteht darin, dass sie Polysaccharide (z. B. Stärke) an den… …   Deutsch Wikipedia

  • Ptyalin — Amylasen sind Enzyme, die bei den meisten Lebewesen vorkommen, und die Polysaccharide abbauen. Heutzutage wird α Amylase auch gentechnisch hergestellt. [1] Ihre Wirkung besteht darin, dass sie Polysaccharide (z. B. Stärke) an den… …   Deutsch Wikipedia

  • Α-Amylase — Amylasen sind Enzyme, die bei den meisten Lebewesen vorkommen, und die Polysaccharide abbauen. Heutzutage wird α Amylase auch gentechnisch hergestellt. [1] Ihre Wirkung besteht darin, dass sie Polysaccharide (z. B. Stärke) an den… …   Deutsch Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”