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Literature summary extracted from

  • Sloane, V.; Waldrop, G.L.
    Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase (2004), J. Biol. Chem., 279, 15772-15778.
    View publication on PubMed

Application

EC Number Application Comment Organism
6.3.4.14 medicine the three biotin carboxylase mutants M169K, R338Q and R338S are used for study in order to mimic the disease-causing mutations M204K and R374Q of propionyl-CoA carboxylase and R385S of 3-methylcrotonyl-CoA carboxylase, which are mutations found in propionic acidemia or methylcrotonylglycinuria patients Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.14 overexpression system Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.14 M169K kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate Escherichia coli
6.3.4.14 N290A active site mutant, negative cooperativity with respect to bicarbonate Escherichia coli
6.3.4.14 R338Q kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate Escherichia coli
6.3.4.14 R338S kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate Escherichia coli
6.4.1.4 M169K mutant with lack of carboxylation activity Escherichia coli
6.4.1.4 R338Q mutant with lack of carboxylation activity Escherichia coli
6.4.1.4 R338S mutant with lack of carboxylation activity Escherichia coli
6.4.1.4 R385S human mutant leading to methylcrotonylglycinuria Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.14 additional information
-
 additional information kinetic data Escherichia coli
6.3.4.14 25
-
 biotin R338S mutant Escherichia coli
6.3.4.14 56
-
 biotin M169K mutant Escherichia coli
6.3.4.14 134
-
 biotin wild-type enzyme Escherichia coli
6.3.4.14 143
-
 biotin R338Q mutant Escherichia coli
6.4.1.4 0.081
-
 ATP
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.14 Mg2+ requirement Escherichia coli
6.4.1.4 Mg2+
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.4.14 50000
-
 2 * 50000, cooperativity between the subunits 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 biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?
6.4.1.4 ATP + acetyl-CoA + HCO3- Escherichia coli
-
 ADP + malonyl-CoA + phosphate
-
 r

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.14
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.14 ADP + carbamoyl phosphate biotin carboxylase catalyzes the formation of ATP from ADP and carbamoyl phosphate Escherichia coli ATP + carbamate
-
 r
6.3.4.14 ATP + biotin + HCO3- utilizes free biotin as substrate Escherichia coli ADP + phosphate + carboxybiotin
-
 r
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, component of the multifunctional acetyl-CoA carboxylase, roles of Arg-338 and Lys-238 in the carboxyl transfer to biotin, Arg-338 serves to orient the carboxyphosphate intermediate for optimal carboxylation of biotin Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 r
6.3.4.14 additional information in absence of biotin enzyme also catalyzes a slow bicarbonate-dependent ATP hydrolysis Escherichia coli ?
-
 ?
6.4.1.4 ATP + acetyl-CoA + HCO3-
-
 Escherichia coli ADP + malonyl-CoA + phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
6.3.4.14 homodimer 2 * 50000, cooperativity between the subunits Escherichia coli
6.4.1.4 homodimer alphabeta Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.4.1.4 MCC
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.14 25
-
 assay at Escherichia coli
6.3.4.14 37
-
 assay at 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 additional information
-
 additional information kinetic data Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.14 8
-
 assay at Escherichia coli