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.
A synthesized peptide derived from human AMY2B, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human A-Myb, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human Amylin, corresponding to a region within the internal amino acids.
AMZ1shares sequence similarity with archaeal metalloproteases called archaemetzincins, but it appears to act predominantly as a basic aminopeptidase. Inhibited by the general metalloprotease inhibitors o-phenanthroline and batimastat. Also significantly inhibited by amastatin, which is an inhibitor of aminopeptidases. Not inhibited by 4-(2-aminoethyl)-benzenesulfonyl fluoride, E-64, and TIMPS (tissue inhibitors of metalloproteinases), which are inhibitors of serine, cysteine, and matrix metalloproteases, respectively.
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