EC Number |
Protein Variants |
Reference |
---|
3.7.1.3 | D132A |
has lower activity and binds pyridoxal 5'-phosphate weakly |
658027 |
3.7.1.3 | D132A |
has lower activity and weaklier pyridoxal-5'-phosphate binding than that of wild-type enzyme |
658027 |
3.7.1.3 | D132A |
mutation results in reduced catalytic activity with L-kynurenine and beta-benzoyl-L-alanine, but not O-benzoyl-L-serine. The mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. The mutant enzyme reacts more slowly with beta-benzoyl-L-alanine and benzaldehyde to form an aldol product absorbing at 490 nm than wild-type |
756117 |
3.7.1.3 | D132E |
has good activity and pyridoxal 5'-phosphate binding stronger than that of the wild-type enzyme |
658027 |
3.7.1.3 | D132E |
has good activity and stronger pyridoxal-5'-phosphate binding than that of wild-type enzyme |
658027 |
3.7.1.3 | D132E |
mutation results in reduced catalytic activity with L-kynurenine and beta-benzoyl-L-alanine, but not O-benzoyl-L-serine. The mutant enzyme can form quinonoid and vinylogous amide intermediates with beta-benzoyl-L-alanine, similar to wild-type enzyme. The mutant enzyme reacts more slowly with beta-benzoyl-L-alanine and benzaldehyde to form an aldol product absorbing at 490 nm than wild-type |
756117 |
3.7.1.3 | D201A |
has very low activity and binds pyridoxal-5'-phosphate weakly, and expresses poorly, giving large amounts of insoluble inclusion bodies and very low levels of soluble protein |
658027 |
3.7.1.3 | D201A |
has very low activity, less than 0.01% of that of the wild-type enzyme, binds pyridoxal 5'-phosphate weakly |
658027 |
3.7.1.3 | D201E |
has good activity and pyridoxal 5'-phosphate binding stronger than that of the wild-type enzyme |
658027 |
3.7.1.3 | D201E |
has good activity and stronger pyridoxal-5'-phosphate binding than that of wild-type enzyme |
658027 |