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 hide
6.3.4.14
-
RECOMMENDED NAME
GeneOntology No.
biotin carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + biotin-carboxyl-carrier protein + HCO3- = ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
biotin biosynthesis
-
-
biotin-carboxyl carrier protein assembly
-
-
SYSTEMATIC NAME
IUBMB Comments
biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9075-71-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene accC
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
gene accC
-
-
Manually annotated by BRENDA team
strain JM109
-
-
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
i.e. Halobacterium halobium, gene accC
UniProt
Manually annotated by BRENDA team
strain DSM 5456/JCM 9403; gene accC
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
-
-
-
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
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
UniProt
Manually annotated by BRENDA team
gene accC
UniProt
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 QLW-P1DMWA-1; gene accC
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Mu50
-
-
Manually annotated by BRENDA team
gene accC
UniProt
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
gene accC
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
-
dimerization of the biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + carbamoyl phosphate
ATP + carbamate
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 + 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
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
2-Pyridyl disulfide
-
-
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
adenosine diphosphopyridoxal
-
ATP, ADP, inorganic phosphate and bicarbonate protect against inhibition
biotin
-
above 300 mM, noncompetitive substrate inhibitor
Co2+
-
above 2 mM
CTP
-
less than 40% residual activity at 20 mM
ethanol
-
maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v
GTP
-
less than 40% residual activity at 20 mM
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
soraphen
soraphen A
Thionucleotides
-
-
-
TTP
-
less than 40% residual activity at 20 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
cyclophilin
cyclophilin stimulates the ATP hydrolysis activity of the enzyme (8fold stimulation of activity at 10fold molar excess over the enzyme)
-
ethanol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.83
ADP
0.081 - 21
ATP
22.7 - 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
62.2
CO2
-
recombinant biotin carboxylase domain of pyruvate carboxylase
0.0076
CoATP2-
-
-
170
D-(+)-biotin
-
-
0.37 - 57.5
HCO3-
0.0398
MgADP-
-
-
0.0546 - 0.11
MgATP2-
0.00126
MnADP-
-
-
0.0025
MnATP2-
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 1.23
ATP
0.0025 - 1.05
biotin
16.68
biotin-carboxyl-carrier protein
Escherichia coli
-
Vmax, C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein
0.0016 - 0.44
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 30C
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
-
7 days old
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
might be associated with the membrane, BC of the undissociated complex acetyl-CoA carboxylase
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / 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)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
LITERATURE
homodimer
monomer
-
mutant enzyme R19E and E23R are monomeric in solution
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a potential 50-amino acid chloroplast transit peptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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 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
-
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
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
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
glycerol protects against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol protects against thermal inactivation
-
the truncated biotin carboxylase domain is more stable than the full-length enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
Ni-NTA column chromatography
nickel affinity chromatography and gel filtration
-
partial
-
partial purification
-
recombinant biotin carboxylase domain of pyruvate carboxylase
-
recombinant 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 srrain BL21-AI by nickel affinity and anion exchange chromatography, and gel filtration
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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recombinant His-tagged enzyme from Escherichia coli strain BL21-AI by nickel affinity chromatography and gel filtration
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recombinant wild-type and mutant His-tagged biotinoyl domains from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration
-
wild-type and mutant enzymes
-
wild-type and mutant, overexpressed BC
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
accA gene, sequencing, expression in Escherichia coli, forms together with accB a two-gene operon
accC gene, overexpression in Escherichia coli
-
expressed in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)pLysS
-
expression of biotin carboxylase domain of acetyl-coenzyme A carboxylase in Escherichia coli
expression of biotin carboxylase domain of pyruvate carboxylase in Escherichia coli
-
expression of the His-tagged biotinoyl domain in Escherichia coli strain AVB101
-
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
gene accC, expression in Escherichia coli srrain BL21-AI as His-tagged enzyme
-
gene accC, expression in Escherichia coli strain BL21-AI as His-tagged enzyme
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gene accC, overexpression in Escherichia coli strain BL21(DE3) as His-tagged enzyme
-
gene encoding a protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein
-
overexpression in Escherichia coli JM109
overexpression system
-
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
E296A
-
50fold decrease in catalytic efficiency, crystallization data
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
H209A
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
H438P
-
decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
I437T
-
decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
K116A
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K238A
-
ATP-binding residue, mutant with much decreased activity, kinetic data
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
R16E
-
the mutant has a 2fold loss in catalytic activity compared with the wild type enzyme. The mutation significantly destabilizes the dimer
R338A
-
250fold decrease in catalytic efficiency
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
R366E
-
mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
R401E
-
mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
E211A
-
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
-
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
-
N290A
-
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
-
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
-
V927A/I931M/M932N/T933Q
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
Show AA Sequence (3231 entries)
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