Increase in activity for the C-terminal Pro-X bond by site-directed mutagenesis of Gly137 to Ala in carboxypeptidase Z.
A mutant carboxypeptidase Z from Absidia zychae in which Gly137 was replaced by Ala by site-directed mutagenesis was constructed and expressed in Saccharomyces cerevisiae YPH250. The mutant enzyme hydrolyzed C-terminal Pro-X bonds (X = amino acid) more efficiently than the wild-type enzyme and sequentially released amino acids from the C-termini of oligopeptides.
Laboratory of Molecular Biology and Microbial Chemistry, Tokyo University of Agriculture and Technology, Japan.
K
K
Ratanakhanokchai
B R
BR
Lee
Y
Y
Kobayashi
M
M
Takeuchi
D000409:Alanine / Q000378:metabolism; D000595:Amino Acid Sequence; D000804:Angiotensin II / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D001920:Bradykinin / Q000378:metabolism; D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism*; D005998:Glycine / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity
D000804:Angiotensin II; D002268:Carboxypeptidases; C022633:serine carboxypeptidase; C499287:carboxypeptidase Z; D000409:Alanine; D001920:Bradykinin; D005998:Glycine