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Information on EC 6.3.4.14 - biotin carboxylase and Organism(s) Escherichia coli and UniProt Accession P24182

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.14 biotin carboxylase
IUBMB Comments
This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin---[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
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This record set is specific for:
Escherichia coli
UNIPROT: P24182
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
biotin carboxylase, accbc, pc-beta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACC
-
-
-
-
BC
-
-
-
-
biotin carboxylase (component of acetyl CoA carboxylase)
-
-
Carboxylase, biotin
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
[biotin carboxyl-carrier protein]-biotin-N6-L-lysine:hydrogencarbonate ligase (ADP-forming)
This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin---[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
CAS REGISTRY NUMBER
COMMENTARY hide
9075-71-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
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 + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
ADP + carbamoyl phosphate
ATP + carbamate
show the reaction diagram
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
show the reaction diagram
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-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
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
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
show the reaction diagram
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
show the reaction diagram
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
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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 + HCO3-
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 + 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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
contains Ca2+
Co2+
-
divalent metal ion required, Mg2+, Mn2+ or Co2+
K+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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-(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
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
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
ATP
ATP shows substrate inhibition which is competitive against bicarbonate
CTP
less than 40% residual activity at 20 mM
GTP
less than 40% residual activity at 20 mM
TTP
less than 40% residual activity at 20 mM
2-Pyridyl disulfide
-
-
adenosine diphosphopyridoxal
-
ATP, ADP, inorganic phosphate and bicarbonate protect against inhibition
ATP
-
the catalytic activity can be inhibited by ATP at high concentrations
biotin
-
above 300 mM, noncompetitive substrate inhibitor
Co2+
-
above 2 mM
ethanol
-
maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v
Mn2+
-
above 2 mM
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
Thionucleotides
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
biotin
ethanol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.093 - 2
ATP
22.7 - 41.8
biotin
1.9 - 57.5
HCO3-
0.00126 - 0.83
ADP
0.0025 - 21
ATP
25 - 1234
biotin
0.16
biotin-carboxyl-carrier protein
-
C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein
0.51 - 11.2
Carbamoyl phosphate
170
D-(+)-biotin
-
-
0.37 - 6.8
HCO3-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.071 - 0.36
ATP
0.0025 - 0.58
biotin
0.0019 - 0.44
HCO3-
0.0012 - 1.23
ATP
0.0037 - 1.05
biotin
16.68
biotin-carboxyl-carrier protein
-
Vmax, C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein
0.0016 - 0.0025
HCO3-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1667 - 3000
ATP
0.00006 - 0.0165
biotin
0.0001 - 162
HCO3-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27
ATP
wild type enzyme, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C
7
Phosphonoacetate
-
-
8
phosphonoacetate linked to the 1'-nitrogen of biotin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000005 - 0.00056
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
0.000028 - 0.0073
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
Mn2+-activated reaction
7.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the biotin carboxylase subunit of acetyl-CoA carboxylase catalyzes the Mg2+-ATP-dependent carboxylation of biotin
physiological function
-
dimerization of the biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
2 * 50000, SDS-PAGE
49320
-
x * 49320, calculation from nucleotide sequence
50000
51000
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
2 * 50000, SDS-PAGE
monomer
mutant enzyme R19E and E23R are monomeric in solution
dimer
homodimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with biotinylated biotin carboxyl carrier protein, sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M Bis-Tris (pH 6.5), and 25% (w/v) PEG 3350
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, using 17% (w/v) PEG3350 and 0.14 M CaCl2, (in complex with two ADP and two Ca2+ ions), or 0.1 M Bis-tris (pH 6.2), 15% (w/v) PEG3350, 0.1 M NH4Cl, and 5% (w/v) n-octyl-beta-D-glucoside (in complex with two ADP and one Mg2+ ion), or 18% (w/v) PEG3350, 0.17 M CsCl, and 4% (v/v) methanol (R16E mutant in complex with bicarbonate and Mg2+-ADP)
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
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-silico docking studies of amino-oxazole inhibitors
-
x-ray structure
-
X-ray structure, native and E288K mutant enzyme, both complexed with ATP
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E288K
inactive active-site mutant
E296A
50fold decrease in catalytic efficiency, crystallization data
F363A
mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is identical to wild-type value
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
R16E
the mutant has a 2fold loss in catalytic activity compared with the wild type enzyme. The mutation significantly destabilizes the dimer
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
R338A
250fold decrease in catalytic efficiency
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
C230A
-
kinetic data, 50fold increased Km for ATP, no effect on the formation of carboxybiotin
E211A
-
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
-
the mutant protein has a kcat value about 30% that of the wild type enzyme
E276Q
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
E288A
-
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
-
the mutant has approximately 84% of the wild type activity
G165V
G165V/G166V
-
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
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K116A
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K116Q
K159Q
K238A
-
ATP-binding residue, mutant with much decreased activity, kinetic data
K238Q
K238R
-
ATP-binding residue, mutant with much decreased activity, kinetic data
M169K
-
kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate
N290A
R19E
-
the mutant has about half the activity of the wild type protein
R292A
R338Q
-
kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate
R338S
-
kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
glycerol protects against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol protects against thermal inactivation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity chromatography and gel filtration
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
-
partial purification
-
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the three biotin carboxylase mutants M169K, R338Q and R338S are used for study in order to mimic the disease-causing mutations M204K and R374Q of propionyl-CoA carboxylase and R385S of 3-methylcrotonyl-CoA carboxylase, which are mutations found in propionic acidemia or methylcrotonylglycinuria patients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tipton, P.A.; Cleland, W.W.
Catalytic mechanism of biotin carboxylase: steady-state kinetic investigation
Biochemistry
27
4317-4325
1988
Escherichia coli
Manually annotated by BRENDA team
Guchhait, R.B.; Polakis, S.E.; Lane, M.D.
Biotin carboxylase component of acetyl-CoA carboxylase from Escherichia coli
Methods Enzymol.
35B
25-31
1975
Escherichia coli
Manually annotated by BRENDA team
Climent, I.; Rubio, V.
ATPase activity of biotin carboxylase provides evidence for initial activation of HCO3- by ATP in the carboxylation of biotin
Arch. Biochem. Biophys.
251
465-470
1986
Escherichia coli
Manually annotated by BRENDA team
Polakis, S.E.; Guchhait, R.B.; Lane, M.D.
On the possible involvement of a carbonyl phosphate intermediate in the adenosine triphosphate-dependent carboxylation of biotin
J. Biol. Chem.
247
1335-1337
1972
Escherichia coli
Manually annotated by BRENDA team
Polakis, S.E.; Guchhait, R.B.; Zwergel, E.E.; Lane, M.D.
Acetyl coenzyme A carboxylase system of Escherichia coli. Studies on the mechanism of the biotin carboxylase- and carboxyltransferase-catalyzed reactions
J. Biol. Chem.
249
6657-6667
1974
Escherichia coli
Manually annotated by BRENDA team
Guchhait, R.B.; Polakis, S.E.; Hollis, D.; Fenselau, C.; Lane, M.D.
Acetyl coenzyme A carboxylase system of Escherichia coli. Site of carboxylation of biotin and enzymatic reactivity of 1'-N-(ureido)-carboxybiotin derivatives
J. Biol. Chem.
24 9
6646-6656
1974
Escherichia coli
Manually annotated by BRENDA team
Guchhait, R.B.; Polakis, S.E.; Dimroth, P.; Stoll, E.; Moss, J.; Lane, M.D.
Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components
J. Biol. Chem.
249
6633-6645
1974
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Dimroth, P.; Guchhait, R.B.; Lane, M.D.
Crystallization of biotin carboxylase, a component enzyme of the acetyl-CoA carboxylase system from Escherichia coli
Hoppe-Seyler's Z. Physiol. Chem.
352
351-354
1971
Escherichia coli
Manually annotated by BRENDA team
Dimroth, P.; Guchhait, R.B.; Stoll, E.; Lane, M.D.
Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase
Proc. Natl. Acad. Sci. USA
67
1353-1360
1970
Escherichia coli
Manually annotated by BRENDA team
Kondo, H.; Shiratsuchi, K.; Yoshimoto, T.; Masuda, T.; Kitazono, A.; Tsuru, D.; Anai, M.; Sekiguchi, M.; Tanabe, T.
Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit
Proc. Natl. Acad. Sci. USA
88
9730-9733
1991
Escherichia coli
Manually annotated by BRENDA team
Li, S.J.; Cronan, J.E.
The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
J. Biol. Chem.
267
855-863
1992
Escherichia coli
Manually annotated by BRENDA team
Waldrop, G.; Holden, H.M.; Rayment, I.
Preliminary X-ray crystallographic analysis of biotin carboxylase isolated from Escherichia coli
J. Mol. Biol.
235
367-369
1994
Escherichia coli
Manually annotated by BRENDA team
Waldrop, G.L.; Rayment, I.; Holden, H.M.
Three-dimensional structure of the biotin carboxylase subunit of the acetyl-CoA carboxylase
Biochemistry
33
10249-10256
1994
Escherichia coli
Manually annotated by BRENDA team
Blanchard, C.Z.; Amspacher, D.; Strongin, R.; Waldrop, G.L.
Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism
Biochem. Biophys. Res. Commun.
266
466-471
1999
Escherichia coli
Manually annotated by BRENDA team
Blanchard, C.Z.; Lee, Y.M.; Frantom, P.A.; Waldrop, G.L.
Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin
Biochemistry
38
3393-3400
1999
Escherichia coli, Escherichia coli JM109
Manually annotated by BRENDA team
Levert, K.L.; Lloyd, R.B.; Waldrop, G.L.
Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?
Biochemistry
39
4122-4128
2000
Escherichia coli
Manually annotated by BRENDA team
Kazuta, Y.; Tokunaga, E.; Aramaki, E.; Kondo, H.
Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue
FEBS Lett.
427
377-380
1998
Escherichia coli
Manually annotated by BRENDA team
Blanchard, C.Z.; Chapman-Smith, A.; Wallace, J.C.; Waldrop, G.L.
The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin
J. Biol. Chem.
274
31767-31769
1999
Escherichia coli
Manually annotated by BRENDA team
Thoden, J.B.; Blanchard, C.Z.; Holden, H.M.; Waldrop, G.L.
Movement of the biotin carboxylase B-domain as a result of ATP binding
J. Biol. Chem.
275
16183-16190
2000
Escherichia coli
Manually annotated by BRENDA team
Sloane, V.; Blanchard, C.Z.; Guillot, F.; Waldrop, G.L.
Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis
J. Biol. Chem.
276
24991-24996
2001
Escherichia coli
Manually annotated by BRENDA team
Janiyani, K.; Bordelon, T.; Waldrop, G.L.; Cronan, J.E., Jr.
Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer
J. Biol. Chem.
276
29864-29870
2001
Escherichia coli
Manually annotated by BRENDA team
Sloane, V.; Waldrop, G.L.
Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase
J. Biol. Chem.
279
15772-15778
2004
Escherichia coli
Manually annotated by BRENDA team
de Queiroz, M.S.; Waldrop, G.L.
Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity
J. Theor. Biol.
246
167-175
2007
Escherichia coli
Manually annotated by BRENDA team
Shen, Y.; Chou, C.Y.; Chang, G.G.; Tong, L.
Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
Mol. Cell
22
807-818
2006
Escherichia coli (P24182), Escherichia coli
Manually annotated by BRENDA team
Nilsson Lill, S.O.; Gao, J.; Waldrop, G.L.
Molecular dynamics simulations of biotin carboxylase
J. Phys. Chem. B
112
3149-3156
2008
Escherichia coli (P24182), Escherichia coli
Manually annotated by BRENDA team
Mochalkin, I.; Miller, J.R.; Evdokimov, A.; Lightle, S.; Yan, C.; Stover, C.K.; Waldrop, G.L.
Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase
Protein Sci.
17
1706-1718
2008
Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Staphylococcus aureus Mu50
Manually annotated by BRENDA team
Lee, C.K.; Cheong, H.K.; Ryu, K.S.; Lee, J.I.; Lee, W.; Jeon, Y.H.; Cheong, C.
Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism
Proteins
72
613-624
2008
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Mochalkin, I.; Miller, J.R.; Narasimhan, L.; Thanabal, V.; Erdman, P.; Cox, P.B.; Prasad, J.V.; Lightle, S.; Huband, M.D.; Stover, C.K.
Discovery of antibacterial biotin carboxylase inhibitors by virtual screening and fragment-based approaches
ACS Chem. Biol.
4
473-483
2009
Moraxella catarrhalis, Haemophilus influenzae, Escherichia coli (P24182)
Manually annotated by BRENDA team
Chou, C.Y.; Yu, L.P.; Tong, L.
Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism
J. Biol. Chem.
284
11690-11697
2009
Escherichia coli (P24182), Escherichia coli
Manually annotated by BRENDA team
Miller, J.R.; Dunham, S.; Mochalkin, I.; Banotai, C.; Bowman, M.; Buist, S.; Dunkle, B.; Hanna, D.; Harwood, H.J.; Huband, M.D.; Karnovsky, A.; Kuhn, M.; Limberakis, C.; Liu, J.Y.; Mehrens, S.; Mueller, W.T.; Narasimhan, L.; Ogden, A.; Ohren, J.; Prasad, J.V.; Shelly, J.A.; Skerlos, L.; Sulavik, M.; Thomas,
A class of selective antibacterials derived from a protein kinase inhibitor pharmacophore
Proc. Natl. Acad. Sci. USA
106
1737-1742
2009
Escherichia coli (P24182)
Manually annotated by BRENDA team
Bordelon, T.; Nilsson Lill, S.; Waldrop, G.
The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase
Proteins Struct. Funct. Bioinform.
74
808-819
2009
Escherichia coli
Manually annotated by BRENDA team
Tong, L.
Structure and function of biotin-dependent carboxylases
Cell. Mol. Life Sci.
70
863-891
2013
Escherichia coli
Manually annotated by BRENDA team
Smith, A.C.; Cronan, J.E.
Dimerization of the bacterial biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo
J. Bacteriol.
194
72-78
2012
Escherichia coli
Manually annotated by BRENDA team
Chou, C.Y.; Tong, L.
Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization
J. Biol. Chem.
286
24417-24425
2011
Escherichia coli (P24182), Escherichia coli
Manually annotated by BRENDA team
Novak, B.; Moldovan, D.; Waldrop, G.; De Queiroz, M.
Behavior of the ATP grasp domain of biotin carboxylase monomers and dimers studied using molecular dynamics simulations
Proteins
79
622-632
2011
Escherichia coli
Manually annotated by BRENDA team
Broussard, T.C.; Kobe, M.J.; Pakhomova, S.; Neau, D.B.; Price, A.E.; Champion, T.S.; Waldrop, G.L.
The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase
Structure
21
650-657
2013
Escherichia coli (P24182), Escherichia coli
Manually annotated by BRENDA team
Brylinski, M.; Waldrop, G.L.
Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries
Molecules
19
4021-4045
2014
Escherichia coli, Haemophilus influenzae, Staphylococcus aureus
Manually annotated by BRENDA team