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Literature summary for 6.4.1.2 extracted from

  • Wei, J.; Tong, L.
    Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer (2015), Nature, 526, 723-727 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.4.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the full-length, 500 kD holoenzyme dimer. The central region contains five domains and is important for positioning the biotin carboxylase and carboxyltransferase domains for catalysis. The structure reveals a dimer of the biotin carboxylase domain Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
K73E mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity Saccharomyces cerevisiae
additional information deletion of the alpha-helical hairpin (alpha8-alpha9, residues 940-972) in domain AC1 or the beta4A-beta4B loop in the C domain of carboxyltransferase (residues 1902-1916) abolishes the catalytic activity Saccharomyces cerevisiae
Q608 mutation has little effect on catalysis Saccharomyces cerevisiae
R656E mutation has little effect on catalysis Saccharomyces cerevisiae
R76E mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity Saccharomyces cerevisiae
W487A mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
soraphen A inhibits the enzyme allosterically by stabilizing a catalytically inactive conformation of the biotin carboxylase domain Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.053
-
 ATP wild-type, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae
0.074
-
 ATP mutant Y83A, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae
0.11
-
 ATP mutant Q608R, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae
0.15
-
 ATP mutant R656E, pH 7.5, temperature not specified in the publication 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 + phosphate + malonyl-CoA
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6
-
 ATP mutant Y83A, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae
5
-
 ATP mutant R656E, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae
8.5
-
 ATP wild-type, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae
16
-
 ATP mutant Q608R, pH 7.5, temperature not specified in the publication Saccharomyces cerevisiae