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Literature summary for 6.4.1.2 extracted from

  • Zhang, H.; Tweel, B.; Tong, L.
    Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop (2004), Proc. Natl. Acad. Sci. USA, 101, 5910-5915.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

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

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 [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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q00955
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetyl-CoA + HCO3-
-
Saccharomyces cerevisiae ADP + malonyl-CoA + phosphate
-
r

Subunits

Subunits Comment Organism
dimer wild-type enzyme, and L1705I and V1967I mutant enzymes, light scattering Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
ACC
-
Saccharomyces cerevisiae
acetyl-coenzyme-A carboxylase
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ADP
-
Saccharomyces cerevisiae
ATP
-
Saccharomyces cerevisiae