EC Number |
Protein Variants |
Reference |
---|
2.4.1.170 | D125A |
in the mutant the kcat is lower and the Km is higher than in wild type enzyme |
674845 |
2.4.1.170 | E376A |
in the mutant the kcat is lower and the Km is higher than in wild type enzyme |
674845 |
2.4.1.170 | E392A |
in the mutant the kcat is lower and the Km is higher than in wild type enzyme |
674845 |
2.4.1.170 | E392D |
in the mutant the kcat is higher and the Km is lower than in wild type enzyme |
674845 |
2.4.1.170 | E456A |
in the mutant the kcat is lower and the Km is slightly lower than in wild type enzyme |
674845 |
2.4.1.170 | H15A |
in the mutant the kcat is lower and the Km is higher than in wild type enzyme |
674845 |
2.4.1.170 | H359A |
in the mutant the kcat is lower and the Km has the same level as in wild type enzyme |
674845 |
2.4.1.170 | H368A |
in the mutant the kcat is higher and the Km is higher than in wild type enzyme |
674845 |
2.4.1.170 | more |
cell engineering by GmIF7GT enzyme coexpression with acyl-CoA carboxylase alpha and beta subunits, biotin ligase, and acetyl-CoA synthetase from Nocardia farcinia for subsequent malonylization of the reaction product of GmIF7GT-encoded isoflavone 7-O-glucosyltransferase. The isoflavonoids are glycosylated at position 7 by 7-O-glycosyltranferase and are further malonylated at position 6' of glucose by malonyl-CoA:isoflavone 7-O-glucoside-6'-O-malonyltransferase both from Glycine max, Scale up for production using a fermentor |
736588 |
2.4.1.170 | more |
Saccharomyces cerevisiae cells expressing PlUGT1 are not able to glycosylate daidzin and puerarin |
736979 |