EC Number   |
Protein Variants |
Reference |
|---|
    2.3.1.94 | C211A |
mutation at the ketosynthase domain active site, exhibits no turnover activity, but is still a competent methylmalonyl-ACP decarboxylase |
756037 |
| 2.3.1.94 | H346A |
mutation at the ketosynthase domain, mutant exhibits reduced rates of both chain translocation and chain elongation, with a greater effect on the latter half-reaction |
756037 |
| 2.3.1.94 | H384A |
mutation at the ketosynthase domain, residue contributes to methylmalonyl-ACP decarboxylation |
756037 |
| 2.3.1.94 | H457A |
activity similar to wild-type |
756037 |
| 2.3.1.94 | K379A |
mutation at the ketosynthase domain, residue promotes C-C bond formation |
756037 |
| 2.3.1.94 | more |
development of expression and purification protocols for subunits DEBS2 and DEBS3 from recombinant strains of Escherichia coli |
736307 |
| 2.3.1.94 | more |
development of mutations that shift the extender unit selectivity of the DEBS terminal module Ery6 (lacking a TE domain) towards either extender unit 2-methylmalonyl-CoA or (prop-2-yn-1-yl)propanedioyl-CoA. Mutants are able to use non-natural alkynyl-modified extender units while maintaining more than twice the activity of the wild-type with its natural substrate |
755678 |
| 2.3.1.94 | more |
site-directed mutagenesis to identify ACP residues that contribute to the observed specificity. Module 3 of the 6-deoxyerythronolide B synthase is reengineered to catalyze two successive rounds of chain elongation |
720991 |
| 2.3.1.94 | N381A |
increase in activity |
756037 |
| 2.3.1.94 | N455L |
activity similar to wild-type |
756037 |
