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Literature summary for 6.3.4.14 extracted from

  • Janiyani, K.; Bordelon, T.; Waldrop, G.L.; Cronan, J.E., Jr.
    Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer (2001), J. Biol. Chem., 276, 29864-29870.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
accC gene, overexpression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
x-ray structure Escherichia coli

Protein Variants

Protein Variants Comment Organism
E288K completely inactive mutant, hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 285fold decreased activity, reduced rate of fatty acid synthesis Escherichia coli
K238Q hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 94fold decreased activity, reduced rate of fatty acid synthesis Escherichia coli
N290A hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 28fold decreased activity, reduced rate of fatty acid synthesis Escherichia coli
R292A hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 39fold decreased activity, reduced rate of fatty acid synthesis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
60.1
-
biotin N290A mutant, homodimer Escherichia coli
64
-
biotin pH 8, 25°C, hybrid dimer K238Q/WT Escherichia coli
123.6
-
biotin R292A mutant, homodimer Escherichia coli
192.7
-
biotin pH 8, 25°C, wild-type enzyme, homodimer Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
2 * 50000, both subunits are required for activity and the two subunits must be in communication during enzyme function Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + biotin-carboxyl-carrier protein + HCO3- Escherichia coli one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to the biotin-carboxyl-carrier protein in vivo, fatty acid synthesis ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
hybrid dimers composed of one subunit having an active site mutation and a second with a wild-type active site Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + HCO3- utilizes free biotin as substrate in vitro Escherichia coli ADP + phosphate + carboxybiotin
-
?
ATP + biotin-carboxyl-carrier protein + HCO3- one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to the biotin-carboxyl-carrier protein in vivo, fatty acid synthesis Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
?
ATP + biotin-carboxyl-carrier protein + HCO3- one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, two complete active sites per homodimer Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 50000, both subunits are required for activity and the two subunits must be in communication during enzyme function Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP ATP-dependent Escherichia coli