EC Number   |
Protein Variants |
Reference |
|---|
    1.2.7.11 | I255V |
kcat/Km for pyruvate is 14% of wild-type value, kcat/KM for 2-oxoglutarate is 38% of wild-type value |
719399 |
| 1.2.7.11 | K125A |
the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme |
718962 |
| 1.2.7.11 | K173A |
the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme |
718962 |
| 1.2.7.11 | K49I |
inactive with 2-oxoglutarate as substrate |
-, 739701 |
| 1.2.7.11 | K49I |
mutant enzyme StOFOR1 with mutation K49I in alpha-subunit. Vmax with pyruvate as substrate is 28% compared to wild-type enzyme, Km with pyruvate as substrate is 2.8fold higher as compared to wild-type enzyme. No activity is detected with 2-oxoglutarate |
-, 739701 |
| 1.2.7.11 | P254G |
kcat/Km for pyruvate is 12% of wild-type value, kcat/KM for 2-oxoglutarate is 20% of wild-type value |
719399 |
| 1.2.7.11 | P257A |
no enzyme activity at either 50 or 80°C |
719399 |
| 1.2.7.11 | P257G |
no enzyme activity at either 50 or 80°C |
719399 |
| 1.2.7.11 | P257V |
no enzyme activity at either 50 or 80°C |
719399 |
| 1.2.7.11 | S41A |
mutant enzyme StOFOR1 with mutation S41A in alpha-subunit. Vmax with pyruvate as substrate is 29% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 40% compared to wild-type enzyme, Km with pyruvate as substrate is 1.5fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.5fold higher as compared to wild-type enzyme |
-, 739701 |
