EC Number |
Protein Variants |
Reference |
---|
2.7.2.8 | D162E |
about 0.1% of wild-type activity |
659704 |
2.7.2.8 | more |
construction of feedback inhibition deregulated Corynebacterium crenatum mutant strains, phenotypes, overview |
-, 738801 |
2.7.2.8 | G11A |
G11A does not hamper recombinant enzyme expression or purification. Mutant shows a 10fold decrease in Vmax values and it selectively increases 8fold the Km for ATP, affecting much less (3fold increase) the apparent Km for N-acetyl-L-glutamate |
722965 |
2.7.2.8 | DELTA25 |
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 17fold increased compared to wild-type |
722087 |
2.7.2.8 | E281A |
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat similar to wild-type, IC50 (L-arginine) 21fold increased compared to wild-type |
722087 |
2.7.2.8 | DELTA2-19 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 148fold increased compared to wild-type |
722087 |
2.7.2.8 | DELTA2-29 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 163fold increased compared to wild-type |
722087 |
2.7.2.8 | DELTA2-15 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 71fold increased compared to wild-type |
722087 |
2.7.2.8 | DELTA8 |
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 16fold increased compared to wild-type |
722087 |
2.7.2.8 | G287A |
Km (N-acetyl-L-glutamate) similar to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 37fold increased compared to wild-type |
722087 |