The active-site and amino-terminal amino acid sequence of bovine intestinal alkaline phosphatase.
The active site of bovine intestinal alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) was labeled with [32P]Pi, a radioactive CNBr peptide was isolated and the amino acid sequence was determined. The sequence of the active-site peptide has limited homology (26%) with the active-site sequence of Escherichia coli alkaline phosphatase except for the ten residues immediately flanking the active-site serine (70%). A possible amino acid sequence deduced from the amino acid composition of an active-site tryptic peptide from human placental alkaline phosphatase is very similar to the bovine intestinal active-site sequence. The amino-terminal sequence of bovine intestinal alkaline phosphatase is homologous (69%) with the human placental enzyme but not with the E. coli phosphatase.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D007422:Intestines / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity
D010446:Peptide Fragments; D000469:Alkaline Phosphatase