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Literature summary for 6.3.4.14 extracted from

  • Shen, Y.; Chou, C.Y.; Chang, G.G.; Tong, L.
    Is dimerization required for the catalytic activity of bacterial biotin carboxylase? (2006), Mol. Cell, 22, 807-818.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion method, crystallization of mutant enzyme E23R and F363A Escherichia coli

Protein Variants

Protein Variants Comment Organism
E23R mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity, mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is 2.6fold lower than wild-type value Escherichia coli
F363A mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is identical to wild-type value Escherichia coli
R19E mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity. kcat/Km for ATP-hydrolysis is 2.5fold lower than wild-type value Escherichia coli
R366E mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP Escherichia coli
R401E mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.093
-
ATP biotin-dependent ATP hydrolysis, mutant enzyme E23R Escherichia coli
0.0948
-
ATP biotin-dependent ATP hydrolysis, mutant enzyme R19E Escherichia coli
0.1049
-
ATP biotin-dependent ATP hydrolysis, mutant enzyme F363A Escherichia coli
0.1152
-
ATP biotin-dependent ATP hydrolysis, wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P24182
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin-carboxyl-carrier protein + CO2
-
Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
?

Subunits

Subunits Comment Organism
dimer wild-type enzyme, dimerization is not an absolute requirement for the catalytic activity of the Escherichia coli biotin carboxylase subunit Escherichia coli
monomer mutant enzyme R19E and E23R are monomeric in solution Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.071
-
ATP biotin-dependent ATP hydrolysis, mutant enzyme E23R Escherichia coli
0.075
-
ATP biotin-dependent ATP hydrolysis, mutant enzyme R19E Escherichia coli
0.207
-
ATP biotin-dependent ATP hydrolysis, mutant enzyme F363A Escherichia coli
0.228
-
ATP biotin-dependent ATP hydrolysis, wild-type enzyme Escherichia coli