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α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]
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 Mb n/a PubMed search n/a Wikidata View/Edit Human Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. This gene is found in many organisms. Amylases are ...
279 11722 Ensembl ENSG00000243480 ENSMUSG00000074264 UniProt P04746 P00687 RefSeq (mRNA) NM_000699 NM_001110505 NM_007446 RefSeq (protein) NP_000690 NP_001103975 NP_031472 Location (UCSC) Chr 1: 103.62 – 103.63 Mb Chr 3: 113.35 – 113.4 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene. Amylases are ...
100043686 Ensembl ENSG00000240038 ENSMUSG00000093931 UniProt P19961 P00688 RefSeq (mRNA) NM_020978 NM_001386109 NM_001387437 NM_001160151 RefSeq (protein) NP_066188 NP_001036176 NP_001153622 NP_001153623 NP_001153624 Location (UCSC) Chr 1: 103.55 – 103.58 Mb Chr 3: 113.22 – 113.23 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Alpha-amylase 2B is an enzyme that in humans is ...
An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid. [10] When used as a food additive, amylase has E number E1100, and may be derived from pig pancreas or mold fungi. Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.
In molecular biology, glycoside hydrolase family 13 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety.
Thus, degrading the biofilm may increase antibiotic efficacy, and potentiate host immune function and healing ability. For example, a combination of alpha-amylase and cellulase was shown to degrade polymicrobial bacterial biofilms from both in vitro and in vivo sources, and increase antibiotic effectiveness against them. [19]
A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases. [3] The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme.