Information on EC 6.3.4.14 - Biotin carboxylase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY
6.3.4.14
-
RECOMMENDED NAME
GeneOntology No.
Biotin carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
carboxylation proceeds via a carboxyphosphate intermediate; MgATP2- and HCO3- add to the enzyme randomly, followed by addition of biotin. Both HCO3- and MgATP2- add in rapid equilibrium
-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
carboxylation proceeds via a carboxyphosphate intermediate
-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
kinetic mechanism
-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
mechanism
-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
reaction mechanism
-
ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
biotin-carboxyl carrier protein assembly
-
Fatty acid biosynthesis
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
Biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ACC
-
-
-
-
AccA
Q9FAF5
Myxococcus xanthus
AccA
Myxococcus xanthus IFO13542/ATCC25232
Q9FAF5
Myxococcus xanthus
-
AccC
F2WMV4
-
BC
-
-
-
-
biotin carboxylase
Q877I5
-
biotin carboxylase
A0RY62
-
biotin carboxylase
A9W9X0
-
biotin carboxylase
-
domain of pyruvate carboxylase
biotin carboxylase
A5G5L1
-
biotin carboxylase
Q9HPP8
-
biotin carboxylase
A2BLY3
-
biotin carboxylase
A4APF1
-
biotin carboxylase
Q8J2Z4
-
biotin carboxylase
-
-
biotin carboxylase
Q3INT5
-
biotin carboxylase
A9A3E8
-
biotin carboxylase
Q3A2P1
-
biotin carboxylase
A1ANN6
-
biotin carboxylase
Polaromonas sp.
Q12EJ0
-
biotin carboxylase
Q12EJ0
-
-
biotin carboxylase
-
domain of acetyl-coenzyme A carboxylase
biotin carboxylase
Q99UY9
component of pyruvate carboxylase
biotin carboxylase
O52602
-
biotin carboxylase
Q97V46
-
biotin carboxylase
-
-
biotin carboxylase
Q54755
-
biotin carboxylase
Q10YA8
-
biotin carboxylase
B1GX36
-
biotin carboxylase (component of acetyl CoA carboxylase)
-
-
biotinoyl domain of acetyl-CoA carboxylase
-
-
PC-beta
-
BC subunit of pyruvate carboxylase
Carboxylase, biotin
-
-
-
-
additional information
-
ATP-grasp superfamily
additional information
-
belongs to the ATP-grasp superfamily
additional information
-
member of the ATP-grasp superfamily
additional information
Escherichia coli JM109
-
member of the ATP-grasp superfamily
-
CAS REGISTRY NUMBER
COMMENTARY
9075-71-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
protein composed of two domains: an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein
-
-
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
gene birA
-
-
Manually annotated by BRENDA team
strain JM109
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
-
-
Manually annotated by BRENDA team
i.e. Halobacterium halobium, gene accC
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
component of pyruvate carboxylase
-
-
Manually annotated by BRENDA team
contains isozymes ACC1 and ACC2
-
-
Manually annotated by BRENDA team
strain DSM 5456/JCM 9403; gene accC
UniProt
Manually annotated by BRENDA team
gene accC
SwissProt
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
a protein possessing a biotin carboxylase function as well as a biotin carrier protein
-
-
Manually annotated by BRENDA team
a protein possessing a biotin carboxylase function as well as a biotin carrier protein
-
-
Manually annotated by BRENDA team
strain IFO13542/ATCC25232
SwissProt
Manually annotated by BRENDA team
Myxococcus xanthus IFO13542/ATCC25232
strain IFO13542/ATCC25232
SwissProt
Manually annotated by BRENDA team
strain DSM 2160/ATCC 35678; gene accC
UniProt
Manually annotated by BRENDA team
transformed with antisense-expression and overexpression tobacco BC constructs, which results in the generation of plants with biotin carboxylase levels ranging from 20 to 500% of the wild-type levels
-
-
Manually annotated by BRENDA team
cv. Little Marvel
-
-
Manually annotated by BRENDA team
Polaromonas sp.
strain JS666/ATCC BAA-500; gene accC
UniProt
Manually annotated by BRENDA team
strain JS666/ATCC BAA-500; gene accC
UniProt
Manually annotated by BRENDA team
strain PAO1
-
-
Manually annotated by BRENDA team
component of pyruvate carboxylase
UniProt
Manually annotated by BRENDA team
strain Mu50
-
-
Manually annotated by BRENDA team
Staphylococcus aureus Mu50
strain Mu50
-
-
Manually annotated by BRENDA team
gene accC
SwissProt
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + carbamoyl phosphate
ATP + carbamate
show the reaction diagram
-
biotin carboxylase catalyzes an ATP synthesis reaction, in which a phosphate group is transferred from carbamoyl phosphate to ADP forming ATP and carbamate
carbamate rapidly decomposes into carbon dioxide and ammonia
-
?
ADP + carbamoyl phosphate
ATP + carbamate
show the reaction diagram
-
biotin carboxylase catalyzes the formation of ATP from ADP and carbamoyl phosphate
-
-
r
ADP + carbamoyl phosphate
ATP + carbamate
show the reaction diagram
Escherichia coli JM109
-
biotin carboxylase catalyzes an ATP synthesis reaction, in which a phosphate group is transferred from carbamoyl phosphate to ADP forming ATP and carbamate
carbamate rapidly decomposes into carbon dioxide and ammonia
-
?
ATP + 1'-N-carboxy-D-biotin + HCO3-
ADP + phosphate + ?
show the reaction diagram
-
the 1'-ureido-N position of biotin is the enzymatic site of carboxylation
-
-
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
-
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
also uses free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
also utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
biotin carboxylase component of the multienzyme complex acetyl-CoA carboxylase, also utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
free biotin, 8000fold lower activity than with the C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein, biotin carboxylase activity of acetyl-CoA carboxylase
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
utilizes free biotin as substrate
-
-
r
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
utilizes free biotin as substrate in vitro
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
Escherichia coli JM109
-
utilizes free biotin as substrate
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
P24182
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q8J2Z4
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
O52602
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q54755
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A1ANN6
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
B1GX36
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A4APF1
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A4SVB6
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Polaromonas sp.
Q12EJ0
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A9W9X0
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A2BLY3
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q3INT5
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q9HPP8
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A9A3E8
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q97V46
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q877I5
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q10YA8
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A5G5L1
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q3A2P1
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A0RY62
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
mathematical modeling and numerical simulations of the kinetics of wild-type, hybrid dimers, and mutant homodimers of biotin carboxylase are performed. Numerical simulations of biotin carboxylase kinetics are the most similar to the experimental data when an oscillating active site model is used. In contrast, alternative models where the active sites are independent do not agree with the experimental data. Thus, the numerical simulations of the proposed kinetic model support the hypothesis that the two active sites of biotin carboxylase alternate their catalytic cycles
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview, biotin is covalently attached to a protein called the biotin-carboxyl-carrier protein. In mammals, these proteins comprise different domains in a single polypeptide chain, biotin must be attached to ACC to produce a functional enzyme
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
in Gram-negative and Gram-positive bacteria biotin carboxylase, carboxyltransferase, and the biotin carboxyl carrier protein are separate proteins
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
the biotinoyl domain interacts with the biotin-carboxyl-carrier protein, BCCP, biotin must be attached to ACC to produce a functional enzyme
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q12EJ0
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Staphylococcus aureus Mu50
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
first half reaction of the first committed step in the biosynthesis of long-chain fatty acids, in vivo the biotin substrate is attached to biotin-carboxyl-carrier protein, natural substrate
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
long-chain fatty acid synthesis, in vivo biotin is covalently attached to the biotin-carboxyl-carrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
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
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
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
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
BC component of the multisubunit complex acetyl-CoA carboxylase, BC catalyzes the ATP-dependent carboxylation of the biotinyl moiety on biotin carboxyl carrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
BC subunit of pyruvate carboxylase, BC/active site structure
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biotin carboxylase component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the first half-reaction of the reaction catalyzed by acetyl-CoA carboxylase, the ATP-dependent carboxylation of biotin, ordered addition of substrates with ATP binding first followed by bicarbonate and then biotin
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biotin carboxylase is one of three distinct components of acetyl-CoA carboxylase, carboxylation of the ureido ring of biotin at the N-1 position, reaction mechanism, domain structure, the biotin carboxylase B-domain moves as a result of ATP binding, enzyme structure
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-, Q9FAF5
biotin carboxylase subunit AccA of acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
Lys-238 interacts with the gamma-phosphate group of ATP but is not involved in catalysis, BC is a subunit of acetyl-CoA carboxylase and mediates the carboxylation of enzyme-bound biotin
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, for that biotin must be deprotonated at its N1 position, mechanism for deprotonation of biotin, bicarbonate is the source of CO2, Lys-238 plays a role in the carboxylation reaction, Cys-230 and Lys-238 do not act as an acid-base pair in the deprotonation of biotin, but may be involved in ATP binding
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, two complete active sites per homodimer
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding and in catalysis orienting ATP in a conformation that allows for optimal catalysis, mechanism
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the first half-reaction of the reaction catalyzed by acetyl-CoA carboxylase, the half-reaction involves the phosphorylation of bicarbonate by ATP to form a carboxyphosphate intermediate, followed by transfer of the carboxyl group to biotin to form carboxybiotin, in vivo biotin is attached to biotin-carboxyl-carrier protein, the C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein form a domain that acts as excellent substrate
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Myxococcus xanthus IFO13542/ATCC25232
Q9FAF5
biotin carboxylase subunit AccA of acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Escherichia coli JM109
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Escherichia coli JM109
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
?
show the reaction diagram
-
the acetyl-CoA carboxylase catalyzes the first commited step in the biosynthesis of long chain fatty acids, the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein
-
-
-
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
-
-
-
-
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
sequential mechanism, in which HCO3- is activated by ATP in a first step
-
-
-
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
L-biotin is completely inactive
-
-
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
-
L-biotin is completely inactive
-
-
-
ATP + d-biotin + HCO3-
ADP + phosphate + carboxy-d-biotin
show the reaction diagram
-
BC component of the multisubunit complex of acetyl-CoA carboxylase
-
-
?
GTP + biotin-carboxyl-carrier protein + HCO3-
GDP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
-
GTP + D-biotin + HCO3-
GDP + phosphate + carboxybiotin
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
enzyme catalyzes ATP-hydrolysis in absence of biotin
-
-
-
additional information
?
-
-, Q9FAF5
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
-
additional information
?
-
-
BC subunit of pyruvate carboxylase, which is involved in gluconeogenesis
-
-
-
additional information
?
-
-
fatty acid synthesis
-
-
-
additional information
?
-
-
long-chain fatty acid synthesis
-
-
-
additional information
?
-
-
pathway from acetyl-CoA to long-chain fatty acids, developmental regulation of enzyme
-
-
-
additional information
?
-
-
biotin carboxylase catalyzes a slow bicarbonate-dependent ATP hydrolysis reaction in the absence of biotin
-
-
-
additional information
?
-
-
in absence of biotin enzyme also catalyzes a slow bicarbonate-dependent ATP hydrolysis
-
-
-
additional information
?
-
-
in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATP hydrolysis at a slow rate
-
-
-
additional information
?
-
-
in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin
-
-
-
additional information
?
-
-
the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase
-
-
-
additional information
?
-
-
active site structure, substrate binding and structure-function relationship analysis, overview
-
-
-
additional information
?
-
-
mechanism of ACC holoenzyme function, structure of the biotinoyl domain of isozyme ACC2, overview
-
-
-
additional information
?
-
-
mechanism of ACC holoenzyme function, structure of the biotinoyl domain, overview. In thei BCCP, Glu 119 and Glu147 interact with the basic residues in BirA, overview
-
-
-
additional information
?
-
-
molecular dynamics simulations of wild-type enzyme and active-site mutant E288K, overview
-
-
-
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q8J2Z4
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
O52602
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q54755
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A1ANN6
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
B1GX36
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A4APF1
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A4SVB6
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Polaromonas sp.
Q12EJ0
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A9W9X0
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A2BLY3
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q3INT5
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q9HPP8
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A9A3E8
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q97V46
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q877I5
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q10YA8
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A5G5L1
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q3A2P1
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
A0RY62
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Q12EJ0
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
-
additional information
?
-
Myxococcus xanthus IFO13542/ATCC25232
Q9FAF5
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
-
additional information
?
-
Escherichia coli JM109
-
in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin
-
-
-
additional information
?
-
Staphylococcus aureus Mu50
-
active site structure, substrate binding and structure-function relationship analysis, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q8J2Z4
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
O52602
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q54755
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A1ANN6
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
B1GX36
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A4APF1
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A4SVB6
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Polaromonas sp.
Q12EJ0
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A9W9X0
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A2BLY3
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q3INT5
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q9HPP8
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A9A3E8
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q97V46
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q877I5
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q10YA8
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A5G5L1
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q3A2P1
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
A0RY62
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Q12EJ0
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Staphylococcus aureus Mu50
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
first half reaction of the first committed step in the biosynthesis of long-chain fatty acids, in vivo the biotin substrate is attached to biotin-carboxyl-carrier protein, natural substrate
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
long-chain fatty acid synthesis, in vivo biotin is covalently attached to the biotin-carboxyl-carrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
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
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
?
show the reaction diagram
-
the acetyl-CoA carboxylase catalyzes the first commited step in the biosynthesis of long chain fatty acids, the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein
-
-
-
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
Escherichia coli JM109
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
additional information
?
-
-, Q9FAF5
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
-
additional information
?
-
-
BC subunit of pyruvate carboxylase, which is involved in gluconeogenesis
-
-
-
additional information
?
-
-
fatty acid synthesis
-
-
-
additional information
?
-
-
long-chain fatty acid synthesis
-
-
-
additional information
?
-
-
pathway from acetyl-CoA to long-chain fatty acids, developmental regulation of enzyme
-
-
-
additional information
?
-
-
the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase
-
-
-
additional information
?
-
Myxococcus xanthus IFO13542/ATCC25232
Q9FAF5
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
structure of the ATP-binding site
ATP
-
ATP-dependent
ATP
-
ATP-dependent, Cys-230 and Lys-238 may be involved in binding ATP
ATP
-
Lys-238 is an ATP-binding residue and interacts with the gamma-phosphate group of ATP, electrostatic interaction
ATP
-
ATP-dependent, mode of binding, Lys-116, His-236 and Glu-201 are involved in binding ATP, the biotin carboxylase B-domain moves as a result of ATP binding
ATP
-
Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding
ATP
Polaromonas sp.
Q12EJ0
-
ATP
-
ATP-dependent
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+
K+
-
required
Mg2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+; Km: 0.57 mM
Mg2+
-
required
Mg2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+
Mg2+
-
requires two equivalents of magnesium for activity
Mg2+
-
requires two equivalents of magnesium for activity, one is complexed to ATP, the role of the other is unknown
Mg2+
Q877I5
-
Mg2+
Polaromonas sp.
Q12EJ0
-
Mg2+
Q54755
-
Mg2+
-
coordinating interactions of active-site metal ions in wild-type and mutant enzymes, Mg2+ is bridged between the alpha- and gamma-phosphoryl group of ATP and coordinated to E288, E276, and a water molecule, detailed overview
Mn2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+; Km: 0.11 mM
Mn2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration above 64 microg per ml for wild-type, 16 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration 8 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration above 64 microg per ml for wild-type, 8 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration 16 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-Pyridyl disulfide
-
-
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
minimal inhibitory concentration 16 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
minimal inhibitory concentration 0.125 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump acrA
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
minimal inhibitory concentration 1 microg per ml for wild-type, 0.5 microg per ml for mutant with targeted knock-out of efflux pump acrA
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse
adenosine diphosphopyridoxal
-
ATP, ADP, inorganic phosphate and bicarbonate protect against inhibition
biotin
-
above 300 mM, noncompetitive substrate inhibitor
Co2+
-
above 2 mM
ethanol
-
maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v
N-ethylmaleimide
-
pH-dependent inhibition, reacts with Lys-238
Phosphonoacetate
-
competitive inhibition versus ATP, noncompetitive versus bicarbonate
phosphonoacetate linked to the 1'-nitrogen of biotin
-
reaction intermediate analog, modest inhibition, competitive versus ATP, noncompetitive versus biotin
soraphen A
Q00955
nanomolar inhibitor against biotin carboxylase domain of acetyl-coenzyme A carboxylase. The inhibitor may bind in the biotin carboxylase dimer interface and inhibits the biotin carboxylase activity by disrupting the oligomerization of the domain
soraphen A
O00763
macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase
Thionucleotides
-
-
-
Mn2+
-
above 2 mM
additional information
-
no substrate inhibition by ATP
-
additional information
-
not inhibited by PLP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
Q99UY9, -
allosteric activator of holoenzyme. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent
biotin
-
required for activation of the ATP synthesis reaction with carbamoyl phosphate and ADP as substrates, E211, E288, N290 and R292 are responsible, at least in part, for the substrate-induced synergism by biotin, activation via a conformational change of enzyme
biotin
-
activates the ATP synthesis reaction with ADP and carbamoyl phosphate as substrates
biotin
-
substrate-induced synergism, the reaction in presence of biotin is 1100fold faster than in its absence
biotin
-
substrate induced synergism, the reaction inpresence of biotin is 1100fold faster than in its absence
biotin
-
substrate-induced synergism, the reaction in presence of biotin is 1100fold faster than in its absence
ethanol
-
maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v
ethanol
-
maximal activation, 11fold at 15%
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
ADP
-
pH 8, 25C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate
0.18
-
ADP
-
pH 8, 25C, E211A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate
0.19
-
ADP
-
pH 8, 25C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate
0.23
-
ADP
-
pH 8, 25C, E288A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate
0.4
-
ADP
-
pH 8, 25C, N290A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate
0.83
-
ADP
-
pH 8, 25C, R292A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate
0.081
-
ATP
-
25C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin
0.093
-
ATP
-
biotin-dependent ATP hydrolysis, mutant enzyme E23R
0.0948
-
ATP
-
biotin-dependent ATP hydrolysis, mutant enzyme R19E
0.1049
-
ATP
-
biotin-dependent ATP hydrolysis, mutant enzyme F363A
0.1152
-
ATP
-
biotin-dependent ATP hydrolysis, wild-type enzyme
0.17
-
ATP
-
wild-type BC
3.3
-
ATP
-
mutant G165V, pH 8.0, 25C
3.4
-
ATP
-
mutant G166V, pH 8.0, 25C
3.8
-
ATP
-
mutant G165V/G166V, pH 8.0, 25C
4.23
-
ATP
-
25C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin
6.87
-
ATP
-
25C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin
8.6
-
ATP
-
K238Q mutant
13
-
ATP
-
K238R mutant
21
-
ATP
-
K238A mutant
22.7
-
biotin
-
pH 7.4, mutant E296A
25
-
biotin
-
R338S mutant
33.6
-
biotin
-
pH 8, 25C, E211A mutant
35.1
-
biotin
-
pH 7.4 wild-type
41.8
-
biotin
-
pH 7.4, mutant R338A
50.9
-
biotin
-
recombinant biotin carboxylase domain of pyruvate carboxylase
56
-
biotin
-
M169K mutant
60.1
-
biotin
-
pH 8, 25C, N290A mutant
60.1
-
biotin
-
N290A mutant, homodimer
64
-
biotin
-
pH 8, 25C, hybrid dimer K238Q/WT
67.6
-
biotin
-
pH 8, 25C, E288A mutant
84.8
-
biotin
-
free biotin
122
-
biotin
-
25C, free biotin, wild-type enzyme
123.6
-
biotin
-
pH 8, 25C, R292A mutant
123.6
-
biotin
-
R292A mutant, homodimer
125
-
biotin
-
pH 8, 25C, K159Q mutant
134
-
biotin
-
-
134
-
biotin
-
pH 8, 25C, wild-type enzyme
134
-
biotin
-
wild-type enzyme
137
-
biotin
-
pH 8, 25C, E276Q mutant
140
-
biotin
-
K238Q mutant
143
-
biotin
-
R338Q mutant
147
-
biotin
-
pH 8, 25C, K116A mutant
160
-
biotin
-
wild-type BC
167
-
biotin
-
25C, free biotin, C230A mutant
180
-
biotin
-
K238A and K238R mutant
186
-
biotin
-
mutant G166V, pH 8.0, 25C
192.7
-
biotin
-
pH 8, 25C, wild-type enzyme, homodimer
256
-
biotin
-
mutant G165V, pH 8.0, 25C
321
-
biotin
-
mutant G165V/G166V, pH 8.0, 25C
1234
-
biotin
-
pH 8, 25C, H209A mutant
0.16
-
biotin-carboxyl-carrier protein
-
C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein
0.51
-
Carbamoyl phosphate
-
pH 8, 25C, E211A mutant, ATP synthesis reaction with ADP as cosubstrate
2.3
-
Carbamoyl phosphate
-
pH 8, 25C, E288A mutant, ATP synthesis reaction with ADP as cosubstrate
2.8
-
Carbamoyl phosphate
-
pH 8, 25C, R292A mutant, ATP synthesis reaction with ADP as cosubstrate
4.8
-
Carbamoyl phosphate
-
pH 8, 25C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate
11.2
-
Carbamoyl phosphate
-
pH 8, 25C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate
62.2
-
CO2
-
recombinant biotin carboxylase domain of pyruvate carboxylase
0.0076
-
CoATP2-
-
-
170
-
D-(+)-biotin
-
-
0.37
-
HCO3-
-
25C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin
0.5
-
HCO3-
-
mutant G165V/G166V, pH 8.0, 25C
0.7
-
HCO3-
-
25C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin
0.8
-
HCO3-
-
mutant G166V, pH 8.0, 25C
1.7
-
HCO3-
-
mutant G165V, pH 8.0, 25C
1.8
-
HCO3-
-
wild-type BC
3.7
-
HCO3-
-
K238A mutant
3.9
-
HCO3-
-
K238Q mutant
6.8
-
HCO3-
-
K238R mutant
16.2
-
HCO3-
-
pH 8.5, wild-type
18.9
-
HCO3-
-
pH 8.5, mutant R338A
57.5
-
HCO3-
-
pH 8.5, mutant E296A
0.0398
-
MgADP-
-
-
0.0546
-
MgATP2-
-
-
0.11
-
MgATP2-
-
-
0.00126
-
MnADP-
-
-
0.0025
-
MnATP2-
-
-
additional information
-
additional information
-
ordered kinetic mechanism
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0012
-
ATP
-
25C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin
0.0017
-
ATP
-
25C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin
0.00195
-
ATP
-
25C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin
0.071
-
ATP
-
biotin-dependent ATP hydrolysis, mutant enzyme E23R
0.075
-
ATP
-
biotin-dependent ATP hydrolysis, mutant enzyme R19E
0.207
-
ATP
-
biotin-dependent ATP hydrolysis, mutant enzyme F363A
0.228
-
ATP
-
biotin-dependent ATP hydrolysis, wild-type enzyme
0.513
-
ATP
-
25C, C230A mutant, biotin-dependent ATP hydrolysis
1.23
-
ATP
-
25C, wild-type enzyme, biotin-dependent ATP hydrolysis
0.0025
-
biotin
-
pH 7.4, mutant R338A
0.0037
-
biotin
-
mutant G166V, pH 8.0, 25C
0.005
-
biotin
-
mutant G165V, pH 8.0, 25C
0.007
-
biotin
-
mutant G165V/G166V, pH 8.0, 25C
0.028
-
biotin
-
pH 7.4, mutant E296A
0.58
-
biotin
-
pH 7.4 wild-type
1.05
-
biotin
-
Vmax, free biotin
16.68
-
biotin-carboxyl-carrier protein
-
Vmax, C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein
0.0016
-
HCO3-
-
mutant G165V/G166V, pH 8.0, 25C; mutant G166V, pH 8.0, 25C
0.0019
-
HCO3-
-
pH 8.5, mutant R338A
0.0025
-
HCO3-
-
mutant G165V, pH 8.0, 25C
0.034
-
HCO3-
-
pH 8.5, mutant E296A
0.44
-
HCO3-
-
pH 8.5, wild-type
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00006
-
biotin
-
pH 7.4, mutant R338A
8026
0.00123
-
biotin
-
pH 7.4, mutant E296A
8026
0.0165
-
biotin
-
pH 7.4 wild-type
8026
0.0001
-
HCO3-
-
pH 8.5, mutant R338A
11306
0.000594
-
HCO3-
-
pH 8.5, mutant E296A
11306
0.0272
-
HCO3-
-
pH 8.5, wild-type
11306
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7
-
Phosphonoacetate
-
-
8
-
phosphonoacetate linked to the 1'-nitrogen of biotin
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000005
-
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
or below, wild-type
0.00016
-
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
mutant H438P
0.00056
-
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
mutant I437T
0.000028
-
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
wild-type
0.0012
-
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
wild-type
0.0073
-
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
wild-type
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
Mn2+-activated reaction
7.3
-
-
assay at
8
-
-
Mg2+-activated reaction
8
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
F2WMV4, -
expression of the accA, accB1, accC and accD genes in Jatropha endosperm varies greatly at different developmental stages. The peak expression of the four genes is observed at about 42 days after fertilization when storage lipids are synthesized at their maximal levels
Manually annotated by BRENDA team
-
developing, 7 days old
Manually annotated by BRENDA team
-
7 days old
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
BC is present in the major plastid compartments envelopes, stroma and thylakoids, but predominantly localized in the stroma, presumably due to partial dissociation as a result of the isolation procedure
Manually annotated by BRENDA team
F2WMV4, -
sequence contains a potential 50-amino acid chloroplast transit peptide
Manually annotated by BRENDA team
-
might be associated with the membrane, BC of the undissociated complex acetyl-CoA carboxylase
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
95000
-
-
gel filtration, analytical ultracentrifugation
additional information
-
-
X-ray model of the enzyme. Those amino acid residues believed to form part of the active site pocket include His209-Glu211, His236-Glu241, Glu276, Ile287-Glu296, and Arg338
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 49320, calculation from nucleotide sequence
?
-
x * 63400, calculation from nucleotide sequence, protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein
?
-, Q9FAF5
x * 61500, sequence calculation, x * 65000, SDS-PAGE
?
-
x * 51000, SDS-PAGE
?
-
x * 64700, recombinant biotin carboxylase domain
?
O52602, -
x * 60000, SDS-PAGE, x * 58235, calculated
?
F2WMV4, -
x * 58300, calculated
?
Myxococcus xanthus IFO13542/ATCC25232
-
x * 61500, sequence calculation, x * 65000, SDS-PAGE
-
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 50000
dimer
-
wild-type enzyme, dimerization is not an absolute requirement for the catalytic activity of the Escherichia coli biotin carboxylase subunit
dimer
Staphylococcus aureus Mu50
-
homodimer
-
homodimer
-
2 * 50000, both subunits are required for activity and the two subunits must be in communication during enzyme function
homodimer
-
2 * 50000, cooperativity between the subunits
homodimer
Escherichia coli JM109
-
2 * 50000
-
monomer
-
mutant enzyme R19E and E23R are monomeric in solution
additional information
-
the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein
additional information
-
geometry of the consensus Met-Lys-Met, MKM, motif, and structure of the biotinoyl domain of BCCP, overview. Binding pattern and interacting surfaces for the biotinoyl domain with BirA, overview
additional information
-
3D structure of the hACC2 biotinoyl domain, geometry of the consensus Met-Lys-Met, MKM, motif, overview. The biotin group of hACC2 does not affect the structure of the biotinoyl domain, the human enzyme does not possess a thumb structure. Binding pattern and interacting surfaces for the ACC2 biotinoyl domain with Escherichia coli BirA enzyme, overview
additional information
F2WMV4, -
biotin carboxylase contains three conserved domains, an N-terminal domain of carbamoyl-phosphate synthase L chain residues 73-181, a ATP binding domain of carbamoyl-phosphate synthase L chain, residues 186-395, and a C-terminal domain of biotin carboxylase
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
F2WMV4, -
sequence contains a potential 50-amino acid chloroplast transit peptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapor-diffusion method, X-ray analysis
-
enzyme in complex with ATP analogues AMP-PNP and ADP-CF2P, hanging drop vapour diffusion, from 0.1 M Bis-Tris, pH 6.5, 0.2 M CaCl2, 45% methylpentanediol, and 10% ethylene glycol or 0.1 M KCl, 3-8% PEG 8000 and 20% ethylene glycol, respectively, X-ray diffraction structure determination and analysis at 2.05 and 2.69 A resolution, respectively, structure modelling
-
in absence and presence of ATP. Upon ATP binding, the central B-domain closes. Residues G165 and G166 play a role in ATP binding
-
in complex with 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
-
sitting-drop vapor diffusion method, crystallization of mutant enzyme E23R and F363A
-
wild-type Escherichia coli biotin carboxylase and mutant E296A in complex with its substrates biotin, bicarbonate, and Mg-ADP, at 2.0 A resolution. Residue Glu296 is the general base that extracts the proton from bicarbonate, and Arg338 is the residue that stabilizes the enolate biotin intermediate in the carboxylation reaction. The B domain of biotin carboxylase is positioned closer to the active site, leading to a 2-A shift in the bound position of the adenine nucleotide and bringing it near the bicarbonate for catalysis. One of the oxygenatoms of bicarbonate is located in the correct position to initiate the nucleophilic attack on ATP to form the carboxyphosphate intermediate. The phosphate group, derived from decomposition of carboxyphosphate, is the general base that extracts the proton on this N1 atom
-
x-ray structure
-
X-ray structure, native and E288K mutant enzyme, both complexed with ATP
-
the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans is crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6 A, b = 116.0 A, c = 115.7 A by hanging-drop vapour-diffusion method. Two biotin carboxylase protomers are contained in the asymmetric unit. Diffraction data are collected at -173C and the crystal structure is solved by the molecular-replacement method and refined against reflections in the 20.02.4 A resolution range
-
crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK
O00763
recombinant apoenzyme or enzyme in complex with ATP analogue AMP-PCP, sitting drop vapour diffusion, from 0.1 M HEPES, pH 7.0, 0.2 M MgCl2, 15-20% PEG 3350, and 10% ethylene glycol in the well solution, X-ray diffraction structure determination and analysis at 2.4 A resolution, structure modelling
-
crystal structure of the recombinant biotin carboxylase domain alone and in complex with soraphen A, sitting drop vapor diffusion method, crystals belong to space group P2(1), with cell parameters of a = 63.83 A, b = 96.52 A, c = 139.95 A and beta = 96.82 A
Q00955
in complex with acetyl-CoA. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent
Q99UY9, -
recombinant enzyme in complex with ATP analogue AMP-PNP, sitting drop vapour diffusion, from 0.2 M KCl, 20% PEG 3350, and 20% ethylene glycol in the well solution, X-ray diffraction structure determination and analysis at 2.10, structure modelling
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
glycerol protects against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol protects against thermal inactivation
-
the truncated biotin carboxylase domain is more stable than the full-length enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme
-
hybrid dimers composed of one subunit having an active site mutation and a second with a wild-type active site
-
native and E288K mutant enzyme
-
recombinant His-tagged biotinoyl domain from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21-AI by nickel affinity chromatography and gel filtration
-
wild-type and mutant enzymes
-
wild-type and mutant, overexpressed BC
-
recombinant biotin carboxylase domain of pyruvate carboxylase
-
recombinant wild-type and mutant His-tagged biotinoyl domains from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration
-
partial
-
recombinant His-tagged enzyme from Escherichia coli srrain BL21-AI by nickel affinity and anion exchange chromatography, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q877I5
overexpression in Escherichia coli JM109
-
expression in Escherichia coli
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A0RY62
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A9W9X0
gene encoding a protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
accC gene, overexpression in Escherichia coli
-
expression in Escherichia coli BL21(DE3)pLysS
-
expression of the His-tagged biotinoyl domain in Escherichia coli strain AVB101
-
gene accC, expression in Escherichia coli strain BL21-AI as His-tagged enzyme
-
overexpression in Escherichia coli JM109
-
overexpression system
-
expression of biotin carboxylase domain of pyruvate carboxylase in Escherichia coli
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A5G5L1
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q9HPP8
expression of wild-type and mutant His-tagged biotinoyl domains in Escherichia coli strain AVB101
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A2BLY3
-
F2WMV4, -
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A4APF1
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q8J2Z4
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
accA gene, sequencing, expression in Escherichia coli, forms together with accB a two-gene operon
-, Q9FAF5
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q3INT5
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A9A3E8
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q3A2P1
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A1ANN6
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Polaromonas sp.
Q12EJ0
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
A4SVB6
expression in Escherichia coli
-
gene accC, expression in Escherichia coli srrain BL21-AI as His-tagged enzyme
-
expression of biotin carboxylase domain of acetyl-coenzyme A carboxylase in Escherichia coli
Q00955
gene accC, overexpression in Escherichia coli strain BL21(DE3) as His-tagged enzyme
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
O52602
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q97V46
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
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gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q54755
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Q10YA8
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
B1GX36
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of the accA, accB1, accC and accD genes in Jatropha endosperm varies greatly at different developmental stages. The peak expression of the four genes is observed at about 42 days after fertilization when storage lipids are synthesized at their maximal levels
F2WMV4, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
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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
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
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mutant with completely abolished ability to hydrolyze ATP
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
E288K
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inactive active-site mutant
E296A
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50fold decrease in catalytic efficiency, crystallization data
F363A
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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
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
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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
H209A
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kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
H438P
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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
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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
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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
K238A
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ATP-binding residue, mutant with much decreased activity, kinetic data
K238Q
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kinetic data, 50fold increased Km for ATP, no formation of carboxybiotin
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
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
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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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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
N290A
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active site mutant, negative cooperativity with respect to bicarbonate
R19E
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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
R338A
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250fold decrease in catalytic efficiency
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
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mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
R401E
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mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
E211A
Escherichia coli JM109
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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
Escherichia coli JM109
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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
Escherichia coli JM109
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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
Escherichia coli JM109
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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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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
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
-, Q9FAF5
accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
additional information
Myxococcus xanthus IFO13542/ATCC25232
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accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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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
medicine
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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