EC Number |
Protein Variants |
Reference |
---|
2.3.2.2 | D433N |
mutation enables gamma-glutamyltranspeptidase to deacylate glutaryl-7-aminocepha-losporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins |
657601 |
2.3.2.2 | D445A |
mutation abolishes transpeptidation activity, specific activity for hydrolysis is 40.2% of that of the wild-type enzyme, salt tolerant like the wild-type enzyme |
658768 |
2.3.2.2 | D445E |
transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity |
658768 |
2.3.2.2 | D445N |
transpeptidation activity is 42% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity |
658768 |
2.3.2.2 | D445Y |
transpeptidation activity is 40% of hydrolysis activity, in wild-type enzyme the transpeptidation activity is 2.38times higher than the hydrolysis activity |
658768 |
2.3.2.2 | F417Y |
site-directed mutagenesis, the mutant shows decreased hydrolysis and increased transfer activity, i.e. gamma-glutamyl-p-nitroanilide hydrolysis and gamma-L-glutamylhydroxamate synthesis, compared to wild-type |
-, 756223 |
2.3.2.2 | G481A |
site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity |
756938 |
2.3.2.2 | G481E |
site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity |
756938 |
2.3.2.2 | G481R |
site-directed mutagenesis, the mutant shows increased catalytic activity, but abolished processing |
756938 |
2.3.2.2 | G482A |
site-directed mutagenesis, the mutant shows increased catalytic activity |
756938 |