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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]
The association of amylase with some drugs has also been reported. [2] The macroamylase molecules are unable to pass through the kidneys and are therefore retained in the blood, leading to elevated levels of amylase in the bloodstream. In contrast, amylase urine levels are normal. [3]
Variations of amylase copy number in dogs mirrors that of human populations, suggesting they acquired the extra copies as they followed humans around. [23] Unlike humans whose amylase levels depend on starch content in diet, wild animals eating a broad range of foods tend to have more copies of amylase.
Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. [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 g
Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene. [ 5 ] [ 6 ] 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.
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 ...
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β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. [ 2 ] [ 3 ] [ 4 ] It catalyses the following reaction: Hydrolysis of (1→4)-α- D -glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains