6.3.4.14: biotin carboxylase
This is an abbreviated version!
For detailed information about biotin carboxylase, go to the full flat file.
Word Map on EC 6.3.4.14
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6.3.4.14
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carboxyltransferase
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carboxylases
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biotin-dependent
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malonyl-coa
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acetyl-coenzyme
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propionyl-coa
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carboxybiotin
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6.4.1.2
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biotin-carboxyl
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biotin-containing
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bicarbonate-dependent
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biotin-binding
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carboxyphosphate
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transcarboxylase
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mgatp-dependent
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accases
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atp-grasp
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medicine
- 6.3.4.14
- carboxyltransferase
- carboxylases
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biotin-dependent
- malonyl-coa
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acetyl-coenzyme
- propionyl-coa
- carboxybiotin
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6.4.1.2
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biotin-carboxyl
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biotin-containing
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bicarbonate-dependent
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biotin-binding
- carboxyphosphate
- transcarboxylase
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mgatp-dependent
- accases
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atp-grasp
- medicine
Reaction
Synonyms
ACC, AccA, AccBC, AccC, BC, biotin carboxylase, biotin carboxylase (component of acetyl CoA carboxylase), biotinoyl domain of acetyl-CoA carboxylase, BirA, Carboxylase, biotin, More, PC-beta
ECTree
6.3.4.14 biotin carboxylaseAdvanced search results
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results (Engineering
Engineering on EC 6.3.4.14 - biotin carboxylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C230A
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kinetic data, 50fold increased Km for ATP, no effect on the formation of carboxybiotin
E211A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
E23R
E276Q
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kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
E288A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
E288K
F363A
G165V
G165V/G166V
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the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold
G166V
H209A
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kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
H438P
decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
I437T
decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
K116A
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kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K116Q
K159Q
K238A
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ATP-binding residue, mutant with much decreased activity, kinetic data
K238Q
K238R
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ATP-binding residue, mutant with much decreased activity, kinetic data
M169K
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kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate
N290A
R16E
the mutant has a 2fold loss in catalytic activity compared with the wild type enzyme. The mutation significantly destabilizes the dimer
R19E
R292A
R338Q
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kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate
R338S
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kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate
R366E
mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
R401E
mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
E211A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
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E288A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
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N290A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
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R292A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
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V927A/I931M/M932N/T933Q
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site-directed mutagenesis, substitution of four amino acids in the vicinity of human MKM motif in analogy to the Escherichia coli biotinylation site
additional information
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
E23R
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the mutant protein has a kcat value about 30% that of the wild type enzyme
E288K
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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
F363A
mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is identical to wild-type value
G165V
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site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows increased Km for ATP and 100fold decreased reaction velocity compared to the wild-type enzyme
G165V
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the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold
G166V
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site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows increased Km for ATP and 100fold decreased reaction velocity compared to the wild-type enzyme
G166V
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the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold
K116Q
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kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K116Q
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site-directed mutagenesis, the phosphate binding site mutant has the residue of the Staphylococcus aureus enzyme and shows a 50fold increased Km for ATP compared to the wild-type enzyme
K159Q
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kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K159Q
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site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows a 90fold higher Km for ATP compared to the wild-type enzyme
K238Q
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ATP-binding residue, mutant with much decreased activity, kinetic data
K238Q
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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
K238Q
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kinetic data, 50fold increased Km for ATP, no formation of carboxybiotin
N290A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
N290A
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active site mutant, negative cooperativity with respect to bicarbonate
N290A
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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
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
R292A
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300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
R292A
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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
R292A
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site-directed mutagenesis, the mutant has a Km for ATP similar to the wild-type enzyme
additional information
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identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive
additional information
accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
additional information
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accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
additional information
Myxococcus xanthus IFO13542 / ATCC 25232
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accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
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