EC Number   |
Protein Variants |
Reference |
|---|
    4.2.1.36 | more |
deletion of enzyme gene, results in almost avirulent mutant cells using a low dose intranasal mouse infection model |
663792 |
| 4.2.1.36 | more |
site-directed mutagenesis of small-subunit HACN protein MJ1271 produces loop-region variant proteins that are reconstituted with wild-type MJ1003 large-subunit protein. The heteromers form promiscuous hydro-lyases with reduced activity but broader substrate specificity, overview |
702368 |
| 4.2.1.36 | more |
small subunit of enzyme, expression in Thermus thermophilus. Gene product functions by forming a heterodimer with LysT subunit of Thermus thermophilus |
664979 |
| 4.2.1.36 | R26K |
site-directed mutagenesis of small-subunit HACN protein MJ1271, the mutant variant forms a relatively efficient IPMI enzyme |
702368 |
| 4.2.1.36 | R26V |
site-directed mutagenesis of small-subunit HACN protein MJ1271, the mutant variant forms a relatively efficient IPMI enzyme. The R26V variant shows detectable dehydratase activity with 3-isopropylmalate |
702368 |
| 4.2.1.36 | R26V/T27Y |
site-directed mutagenesis of small-subunit HACN protein MJ1271, the mutant variant resembles the MJ1277 IPMI small subunit in its flexible loop sequence but demonstrates the broad substrate specificity of theR26V variant |
702368 |
| 4.2.1.36 | T27A |
site-directed mutagenesis of small-subunit HACN protein MJ1271, the mutant variant has uniformly lower specificity constants for both IPMI and HACN substrates compared to the wild-type enzyme. In a holoenzyme complex, the T27A variant catalyzes the hydration of citraconate and maleate substrates with a 10fold higher KM than wild-type IPMIMj, and the KM values for cis-homoaconitate substrates increase 10-20fold relative to the wild-type HACNMj. The T27A variant has no detectable dehydratase activity with 3-isopropylmalate |
702368 |
