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{{Infobox_gene}}
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'''Pancreatic alpha-amylase''' is an [[enzyme]] that in humans is encoded by the ''AMY2A'' [[gene]].<ref name="pmid3260028">{{cite journal | vauthors = Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR | title = Human pancreatic amylase is encoded by two different genes | journal = Nucleic Acids Res | volume = 16 | issue = 10 | pages = 4724 |date=Jul 1988 | pmid = 3260028 | pmc = 336663 | doi =10.1093/nar/16.10.4724 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AMY2A amylase, alpha 2A; pancreatic| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=279| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_AMY2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b2y.
| PDB = {{PDB2|1b2y}}, {{PDB2|1bsi}}, {{PDB2|1c8q}}, {{PDB2|1cpu}}, {{PDB2|1hny}}, {{PDB2|1jxj}}, {{PDB2|1jxk}}, {{PDB2|1kb3}}, {{PDB2|1kbb}}, {{PDB2|1kbk}}, {{PDB2|1kgu}}, {{PDB2|1kgw}}, {{PDB2|1kgx}}, {{PDB2|1mfu}}, {{PDB2|1mfv}}, {{PDB2|1nm9}}, {{PDB2|1q4n}}, {{PDB2|1smd}}, {{PDB2|1u2y}}, {{PDB2|1u30}}, {{PDB2|1u33}}, {{PDB2|1xcw}}, {{PDB2|1xcx}}, {{PDB2|1xd0}}, {{PDB2|1xd1}}, {{PDB2|1xgz}}, {{PDB2|1xh0}}, {{PDB2|1xh1}}, {{PDB2|1xh2}}, {{PDB2|1xv8}}, {{PDB2|1z32}}, {{PDB2|2cpu}}, {{PDB2|3cpu}}
| Name = Amylase, alpha 2A; pancreatic
| HGNCid = 477
| Symbol = AMY2A
| AltSymbols =; AMY2; AMY2B; PA
| OMIM = 104650
| ECnumber = 
| Homologene = 20179
| MGIid = 88019
| Function = {{GNF_GO|id=GO:0004556 |text = alpha-amylase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
  | Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 279
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_000690
    | Hs_RefseqmRNA = NM_000699
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 11722
    | Mm_Ensembl = ENSMUSG00000074264
    | Mm_RefseqmRNA = NM_007446
    | Mm_RefseqProtein = NP_031472
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 113547957
    | Mm_GenLoc_end = 113569751
    | Mm_Uniprot = Q921Y7
  }}
}}
'''Amylase, alpha 2A; pancreatic''', also known as '''AMY2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMY2A amylase, alpha 2A; pancreatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=279| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 pancreas.<ref name="entrez">{{cite web | title = Entrez Gene: AMY2A amylase, alpha 2A; pancreatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=279| accessdate = }}</ref>
| 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 pancreas.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|AMY2A}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Kaczmarek MJ, Rosenmund H |title=The action of human pancreatic and salivary isoamylases on starch and glycogen. |journal=Clin. Chim. Acta |volume=79 |issue= 1 |pages= 69-73 |year= 1977 |pmid= 890964 |doi=  }}
*{{cite journal  | vauthors=Kaczmarek MJ, Rosenmund H |title=The action of human pancreatic and salivary isoamylases on starch and glycogen |journal=Clin. Chim. Acta |volume=79 |issue= 1 |pages= 69–73 |year= 1977 |pmid= 890964 |doi=10.1016/0009-8981(77)90462-4 }}
*{{cite journal  | author=Jacob M, Lainé J, LeBel D |title=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. |journal=Biochem. Cell Biol. |volume=70 |issue= 10-11 |pages= 1105-14 |year= 1993 |pmid= 1284286 |doi=  }}
*{{cite journal  | vauthors=Jacob M, Lainé J, LeBel D |title=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 |journal=Biochem. Cell Biol. |volume=70 |issue= 10–11 |pages= 1105–14 |year= 1993 |pmid= 1284286 |doi=10.1139/o92-156 }}
*{{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  | vauthors=Groot PC, Mager WH, Henriquez NV |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=10.1016/0888-7543(90)90230-R |display-authors=etal}}
*{{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  | vauthors=Nishide T, Nakamura Y, Emi M |title=Primary structure of human salivary alpha-amylase gene |journal=Gene |volume=41 |issue= 2–3 |pages= 299–304 |year= 1986 |pmid= 2423416 |doi=10.1016/0378-1119(86)90110-1  |display-authors=etal}}
*{{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  | vauthors=Horii A, Emi M, Tomita N |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=10.1016/0378-1119(87)90213-7 |display-authors=etal}}
*{{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  | vauthors=Gumucio DL, Wiebauer K, Caldwell RM |title=Concerted evolution of human amylase genes |journal=Mol. Cell. Biol. |volume=8 |issue= 3 |pages= 1197–205 |year= 1988 |pmid= 2452973 |doi=  | pmc=363264  |display-authors=etal}}
*{{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  | vauthors=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=10.1093/nar/16.17.8261  | pmc=338557  }}
*{{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  | vauthors=Groot PC, Bleeker MJ, Pronk JC |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=10.1016/0888-7543(89)90083-9 |display-authors=etal}}
*{{cite journal  | author=Groot PC, Bleeker MJ, Pronk JC, ''et al.'' |title=Human pancreatic amylase is encoded by two different genes. |journal=Nucleic Acids Res. |volume=16 |issue= 10 |pages= 4724 |year= 1988 |pmid= 3260028 |doi=  }}
*{{cite journal  | vauthors=Wise RJ, Karn RC, Larsen SH |title=A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A |journal=Mol. Biol. Med. |volume=2 |issue= 5 |pages= 307–22 |year= 1986 |pmid= 6336237 |doi=  |display-authors=etal}}
*{{cite journal  | author=Wise RJ, Karn RC, Larsen SH, ''et al.'' |title=A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A. |journal=Mol. Biol. Med. |volume=2 |issue= 5 |pages= 307-22 |year= 1986 |pmid= 6336237 |doi=  }}
*{{cite journal  | vauthors=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=10.1007/BF01534909 }}
*{{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  | vauthors=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=10.1016/0378-1119(84)90265-8  }}
*{{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  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Qian M, Haser R, Buisson G |title=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 |journal=Biochemistry |volume=33 |issue= 20 |pages= 6284–94 |year= 1994 |pmid= 8193143 |doi=10.1021/bi00186a031 |display-authors=etal}}
*{{cite journal  | author=Qian M, Haser R, Buisson G, ''et al.'' |title=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. |journal=Biochemistry |volume=33 |issue= 20 |pages= 6284-94 |year= 1994 |pmid= 8193143 |doi=  }}
*{{cite journal  | vauthors=Brayer GD, Luo Y, Withers SG |title=The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes |journal=Protein Sci. |volume=4 |issue= 9 |pages= 1730–42 |year= 1996 |pmid= 8528071 |doi=10.1002/pro.5560040908  | pmc=2143216 }}
*{{cite journal  | author=Brayer GD, Luo Y, Withers SG |title=The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. |journal=Protein Sci. |volume=4 |issue= 9 |pages= 1730-42 |year= 1996 |pmid= 8528071 |doi= }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | vauthors=Rydberg EH, Sidhu G, Vo HC |title=Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris |journal=Protein Sci. |volume=8 |issue= 3 |pages= 635–43 |year= 1999 |pmid= 10091666 |doi=10.1110/ps.8.3.635  | pmc=2144294 |display-authors=etal}}
*{{cite journal  | author=Rydberg EH, Sidhu G, Vo HC, ''et al.'' |title=Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. |journal=Protein Sci. |volume=8 |issue= 3 |pages= 635-43 |year= 1999 |pmid= 10091666 |doi=  }}
*{{cite journal  | vauthors=Brayer GD, Sidhu G, Maurus R |title=Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques |journal=Biochemistry |volume=39 |issue= 16 |pages= 4778–91 |year= 2000 |pmid= 10769135 |doi=10.1021/bi9921182 |display-authors=etal}}
*{{cite journal  | author=Brayer GD, Sidhu G, Maurus R, ''et al.'' |title=Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. |journal=Biochemistry |volume=39 |issue= 16 |pages= 4778-91 |year= 2000 |pmid= 10769135 |doi=  }}
*{{cite journal  | author=Aughsteen AA |title=A comparative immunohistochemical study on amylase localization in the rat and human exocrine pancreas |journal=Saudi medical journal |volume=22 |issue= 5 |pages= 410–5 |year= 2001 |pmid= 11376382 |doi=  }}
*{{cite journal  | author=Aughsteen AA |title=A comparative immunohistochemical study on amylase localization in the rat and human exocrine pancreas. |journal=Saudi medical journal |volume=22 |issue= 5 |pages= 410-5 |year= 2001 |pmid= 11376382 |doi= }}
*{{cite journal  | vauthors=Numao S, Maurus R, Sidhu G |title=Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase |journal=Biochemistry |volume=41 |issue= 1 |pages= 215–25 |year= 2002 |pmid= 11772019 |doi=10.1021/bi0115636 |display-authors=etal}}
*{{cite journal | author=Numao S, Maurus R, Sidhu G, ''et al.'' |title=Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase. |journal=Biochemistry |volume=41 |issue= 1 |pages= 215-25 |year= 2002 |pmid= 11772019 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=279}}
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Revision as of 01:56, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. 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. 2.0 2.1 "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic".

External links

Further reading