EC Number   |
Protein Variants |
Reference |
|---|
   5.4.99.13 | F598A |
site-directed mutagenesis, the mutation causes a 17fold increase in catalytic efficiency in pivalyl-CoA mutase activity and a concomitant about 240fold decrease in isobutyryl-CoA mutase activity compared to wild-type IcmF. The mutation of the single residue in IcmF tunes the substrate specificity to an about 4000fold increase in the specificity for the unnatural substrate. The F598A mutant is more susceptible to inactivation than wild-type IcmF |
-, 748193 |
| 5.4.99.13 | F598G |
site-directed mutagenesis, inactive mutant |
-, 748193 |
| 5.4.99.13 | F598I |
site-directed mutagenesis, the isobutyryl-CoA mutase activity of the mutant is diminished and the isovaleryl-CoA mutase activity is increased compared to wild-type |
-, 748193 |
| 5.4.99.13 | F598L |
site-directed mutagenesis, the isobutyryl-CoA mutase activity of the mutant is diminished and the isovaleryl-CoA mutase activity is increased compared to wild-type |
748193 |
| 5.4.99.13 | F598V |
site-directed mutagenesis, the isobutyryl-CoA mutase activity of the mutant is diminished and the isovaleryl-CoA mutase activity is increased compared to wild-type |
748193 |
| 5.4.99.13 | more |
AdoCbl is quantitatively converted to cob(II)alamin when isovaleryl-CoA is added to F598A or to the F598I/L or Q742A mutants inactivating the enzyme, The F598A mutant inactivates 3fold more rapidly than wild-type IcmF |
-, 748193 |
| 5.4.99.13 | more |
disruption of IcmA in Streptomyces cinnamonensis |
648803 |
| 5.4.99.13 | more |
engineering of enzyme IcmF to increase pivalyl-CoA mutase activityby targeting two active site residues predicted to be key to substrate selectivity based on sequence alignments and crystal structures. PCM-F is an artificially engineered variant of PCM (IcmF) in which the large and small subunits are fused via an 11-amino acid linker |
-, 748193 |
| 5.4.99.13 | more |
the production of isobutanol, a branched-chain alcohol that can be used as a gasoline substitute, using a CoA-dependent pathway in recombinant Ralstonia eutropha strain H16. The designed pathway is constituted of three modules: chain elongation, rearrangement, and modification. First, the chain elongation and modification modules are integrated and optimized, esulting in the production of about 200 mg/l n-butanol from fructose or 30 mg/L from formate by engineered Ralstonia eutropha. Subsequently, the rearrangement module is incorporated, featuring native isobutyryl-CoA mutase in Ralstonia eutropha. The engineered strain produces about 30 mg/l isobutanol from fructose. The demonstrated carbon skeleton rearrangement chemistry may be used to expand the range of the chemicals accessible with CoA-dependent pathways |
746607 |
| 5.4.99.13 | Q742A |
site-directed mutagenesis, the mutant shows undetectable isovaleryl-CoA mutase activity and significantly diminished isobutyryl-CoA mutase activity compared to wild-type |
748193 |
