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Literature summary extracted from

  • Chou, C.Y.; Tong, L.
    Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization (2011), J. Biol. Chem., 286, 24417-24425.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.14 sitting drop vapor diffusion method, using 17% (w/v) PEG3350 and 0.14 M CaCl2, (in complex with two ADP and two Ca2+ ions), or 0.1 M Bis-tris (pH 6.2), 15% (w/v) PEG3350, 0.1 M NH4Cl, and 5% (w/v) n-octyl-beta-D-glucoside (in complex with two ADP and one Mg2+ ion), or 18% (w/v) PEG3350, 0.17 M CsCl, and 4% (v/v) methanol (R16E mutant in complex with bicarbonate and Mg2+-ADP) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.14 R16E the mutant has a 2fold loss in catalytic activity compared with the wild type enzyme. The mutation significantly destabilizes the dimer Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.4.14 ADP
-
 Escherichia coli
6.3.4.14 ATP ATP shows substrate inhibition which is competitive against bicarbonate Escherichia coli
6.3.4.14 CTP less than 40% residual activity at 20 mM Escherichia coli
6.3.4.14 GTP less than 40% residual activity at 20 mM Escherichia coli
6.3.4.14 TTP less than 40% residual activity at 20 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.14 0.1 2 ATP mutant enzyme R16E, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli
6.3.4.14 0.1 2 ATP wild type enzyme, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli
6.3.4.14 1.9
-
 HCO3- wild type enzyme, with 1.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 5
-
 HCO3- wild type enzyme, with 7.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 6.5
-
 HCO3- wild type enzyme, with 10 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 11.4
-
 HCO3- wild type enzyme, with 20 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.14 Ca2+ contains Ca2+ Escherichia coli
6.3.4.14 Mg2+ dependent on Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- Escherichia coli
-
 ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.14 Escherichia coli P24182
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3-
-
 Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.14 dimer
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.4.14 0.2
-
 ATP mutant enzyme R16E, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli
6.3.4.14 0.3
-
 HCO3- wild type enzyme, with 20 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 0.31
-
 HCO3- wild type enzyme, with 1.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 0.32
-
 HCO3- wild type enzyme, with 10 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 0.36
-
 ATP wild type enzyme, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli
6.3.4.14 0.36
-
 HCO3- wild type enzyme, with 7.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.14 ATP
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.3.4.14 27
-
 ATP wild type enzyme, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli

General Information

EC Number General Information Comment Organism
6.3.4.14 metabolism the biotin carboxylase subunit of acetyl-CoA carboxylase catalyzes the Mg2+-ATP-dependent carboxylation of biotin Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.4.14 26
-
 HCO3- wild type enzyme, with 20 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 49
-
 HCO3- wild type enzyme, with 10 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 71
-
 HCO3- wild type enzyme, with 7.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 162
-
 HCO3- wild type enzyme, with 1.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C Escherichia coli
6.3.4.14 1667
-
 ATP mutant enzyme R16E, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli
6.3.4.14 3000
-
 ATP wild type enzyme, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C Escherichia coli