Crystallization (Comment) | Organism |
---|---|
purified wild-type enzyme and mutant enzymes, free or in complex with inhibitors haloxyfop or diclofop, 10 mg/ml protein with reservoir solution containing 0.1 M sodium citrate, pH 5.5, 0.2 M NaCl, 8% w/v PEG 8000, and 10% v/v glycerol, complexing by soaking of crystals in 5 mM inhibitor solution, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.5-2.8 A resolution | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
L1705I | site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme | Saccharomyces cerevisiae |
L1705I/V1967I | site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme | Saccharomyces cerevisiae |
V1967I | site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Diclofop | herbicide, molecular inhibition mechanism, active site binding structure involving Tyr1738 and Phe1956, binding induces large conformational changes in the enzyme | Saccharomyces cerevisiae | |
Haloxyfop | herbicide, molecular inhibition mechanism, active site binding structure involving Tyr1738 and Phe1956, binding induces large conformational changes in the enzyme | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of recombinant wild-type and mutant enzymes | Saccharomyces cerevisiae | |
0.075 | - |
malonyl-CoA | pH 8.0, recombinant wild-type enzyme | Saccharomyces cerevisiae | |
0.75 | - |
malonyl-CoA | pH 8.0, recombinant mutant enzymes | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q00955 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + acetyl-CoA + HCO3- | - |
Saccharomyces cerevisiae | ADP + malonyl-CoA + phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | wild-type enzyme, and L1705I and V1967I mutant enzymes, light scattering | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
ACC | - |
Saccharomyces cerevisiae |
acetyl-coenzyme-A carboxylase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Saccharomyces cerevisiae | |
ATP | - |
Saccharomyces cerevisiae |