Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1Agene.[3] This gene is found in many organisms.
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]
Overview of all the structural information available in the PDB for UniProt: P04745 (Alpha-amylase 1) at the PDBe-KB.[dead link]
Further reading
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. PMID1710976. S2CID27328712.
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. PMID2081604.
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. PMID2423416.
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. PMID2424823.
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. PMID2442579.
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. PMID2450054.
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. PMID2788608.
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. PMID6176528. S2CID37322144.
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. PMID6608795. S2CID21230969.
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. PMID6610603.
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. PMID7507116. S2CID6897149.
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. PMID11858714.
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. PMID12104089.
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. PMID12527308.
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