Crystallization (Comment) | Organism |
---|---|
enzyme in complex with inhibitor CoA methyldisulfide | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CoA methyldisulfide | CoA methyldisulfide shows rapid inhibition of one monomer of FabH through formation of a methyl disulfide conjugate. Reaction of the second subunit with either MeSSCoA or acetyl-CoA is much slower. In the presence of malonyl-ACP, the acylation rate of the second subunit is restored to that of the native FabH | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6R0 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
FabH | - |
Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0571 | - |
pH 7.4, 23°C | Escherichia coli | CoA methyldisulfide |
General Information | Comment | Organism |
---|---|---|
metabolism | catalytic model, a structurally disordered apo-ecFabH dimer orders on binding either the first substrate, acetyl-CoA, or the inhibitor MeSSCoA, and is restored to a disordered state on binding of malonyl-ACP | Escherichia coli |