AMY2B

Amylase, alpha 2B (pancreatic)

PDB rendering based on 1b2y.

Available structures
PDB	1b2y, 1bsi, 1c8q, 1cpu, 1hny, 1jxj, 1jxk, 1kb3, 1kbb, 1kbk, 1kgu, 1kgw, 1kgx, 1mfu, 1mfv, 1nm9, 1q4n, 1smd, 1u2y, 1u30, 1u33, 1xcw, 1xcx, 1xd0, 1xd1, 1xgz, 1xh0, 1xh1, 1xh2, 1xv8, 1z32, 2cpu, 3cpu

Identifiers

Symbols

AMY2B; AMY2

External IDs

OMIM: 104660 HomoloGene: 117989 GeneCards: AMY2B Gene

EC number

3.2.1.1

Gene Ontology
Molecular function	• alpha-amylase activity • hydrolase activity, acting on glycosyl bonds • metal ion binding
Cellular component	• extracellular region
Biological process	• carbohydrate metabolic process • digestion
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_020978

n/a

RefSeq (protein)

NP_066188

n/a

Location (UCSC)

Chr 1:
104.1 – 104.12 Mb

n/a

PubMed search

[1]

n/a

Alpha-amylase 2B is an enzyme that in humans is encoded by the AMY2B 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

^ Omichi K, Hase S (Jan 1994). "Identification of the characteristic amino-acid sequence for human alpha-amylase encoded by the AMY2B gene". Biochim Biophys Acta 1203 (2): 224–9. PMID 8268204.
^ ^a ^b "Entrez Gene: AMY2B amylase, alpha 2B (pancreatic)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=280.

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.
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.
Yokouchi H, Horii A, Emi M, et al. (1990). "Cloning and characterization of a third type of human alpha-amylase gene, AMY2B.". Gene 90 (2): 281–6. doi:10.1016/0378-1119(90)90191-S. PMID 2401405.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=363264.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=338557.
Tomita N, Horii A, Doi S, et al. (1989). "A novel type of human alpha-amylase produced in lung carcinoid tumor.". Gene 76 (1): 11–8. doi:10.1016/0378-1119(89)90003-6. PMID 2701942.
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.
Groot PC, Bleeker MJ, Pronk JC, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=336663.
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.
Nagase T, Nakayama M, Nakajima D, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 8 (2): 85–95. doi:10.1093/dnares/8.2.85. PMID 11347906.
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.
Koyama I, Komine S, Iino N, et al. (2001). "alpha-Amylase expressed in human liver is encoded by the AMY-2B gene identified in tumorous tissues.". Clin. Chim. Acta 309 (1): 73–83. doi:10.1016/S0009-8981(01)00501-0. PMID 11408008.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Iafrate AJ, Feuk L, Rivera MN, et al. (2004). "Detection of large-scale variation in the human genome.". Nat. Genet. 36 (9): 949–51. doi:10.1038/ng1416. PMID 15286789.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.

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 ethe mobile loop in the mehanism 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

AMY2B

References

Further reading