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Information on EC 6.3.4.15 - biotin-[biotin carboxyl-carrier protein] ligase
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6.3.4.15 biotin-[biotin carboxyl-carrier protein] ligaseIUBMB Comments
The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14, biotin carboxylase. The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15, acetyl-CoA carboxytransferase. In some organisms the carrier protein is part of EC 6.4.1.2, acetyl-CoA carboxylase.
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Word Map
- 6.3.4.15
-
biotinylation
- streptavidin
-
bioid
-
proximity-dependent
- bap
- avidin
-
avitag
-
streptavidin-coated
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biotin-dependent
- transcarboxylase
-
proximity-labeling
-
biotinyl-5\'-amp
- drug development
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unbiotinylated
-
15-amino
-
biotin-streptavidin
- diagnostics
- analysis
- synthesis
- carboxylases
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
biotin ligase, bira protein, biotin-protein ligase, biotin holoenzyme synthetase, bacterial bira biotin ligase, biotin acetyl-coa carboxylase ligase, group i biotin protein ligase, biotin:apocarboxylase ligase, holocarboxylase synthetase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acetyl CoA holocarboxylase synthetase
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-
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Acetyl coenzyme A holocarboxylase synthetase
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-
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Biotin holoenzyme synthetase
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-
-
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biotin ligase
biotin protein ligase
Biotin--protein ligase
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-
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biotin-protein ligase
Biotin-[acetyl coenzyme A carboxylase] synthetase
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-
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Biotin-[acetyl-CoA carboxylase] synthetase
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Biotin:apocarboxylase ligase
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-
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BirA
BPL
HCS
Holocarboxylase synthetase
STK_15250
Synthetase, biotin-[acetyl coenzyme A carboxylase]
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-
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additional information
BirA
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BirA
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bifunctional protein, catalyzes post-translational biotin addition to a biotin-dependent carboxylase and binds sequence-specifically to DNA to repress transcription initiation at the biotin biosynthetic operon
HCS
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-
-
-
Holocarboxylase synthetase
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-
additional information
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the BPL of Mycobacterium tuberculosis belongs to the group I enzymes, monofunctional enzymes lacking the N-terminal HTH domain
additional information
the enzyme belongs to the biotin-dependent acetyl-CoA carboxylases/transcarboxylases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
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-
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ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
reaction mechanism involving Lys111, formation of a biotinyl-5'-AMP intermediate, active site structure, ligand binding to the active site loop, overview
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ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
reaction mechanism, the first step is the reversible formation of a biotinyl-5'-AMP intermediate followed by irreversible transfer of the biotinyl group to the protein
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ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
reaction mechanism involving Lys111, formation of a biotinyl-5'-AMP intermediate, active site structure, ligand binding to the active site loop, overview
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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-
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carboxylic acid formation
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carboxamide formation
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additional information
biotinylation, mediates attachment of biotin to a fusion protein of a biotin acceptor peptide and GLuc, EC 1.13.12.5
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SYSTEMATIC NAME
IUBMB Comments
biotin:apo-[carboxyl-carrier protein] ligase (AMP-forming)
The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14, biotin carboxylase. The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15, acetyl-CoA carboxytransferase. In some organisms the carrier protein is part of EC 6.4.1.2, acetyl-CoA carboxylase.
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CAS REGISTRY NUMBER
COMMENTARY
37340-95-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4S)-4-(hept-6-yn-1-yl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one + 9-(4-azidobutyl)-9H-purin-6-amine
(4S)-4-(5-[1-[4-(6-amino-9H-purin-9-yl)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
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i.e. reaction of acetylene derivative of biotin and an azide-functionalized adenine
-
-
?
(4S)-4-(hept-6-yn-1-yl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one + N-(3-azidopropyl)-7-nitro-2,1,3-benzoxadiazol-4-amine
(4S)-4-[5-(1-[3-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]propyl]-1H-1,2,3-triazol-4-yl)pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
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i.e. reaction of acetylene derivative of biotin and an azide-functionalied analogue of the fluorophore nitrobenzofurazan
-
-
?
ATP + biotin + apo-[acetyl CoA carboxylase]
AMP + diphosphate + acetyl CoA carboxylase
no coupling is observed in ATP and biotin binding to the BPL
-
-
?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
ATP + biotin + apo-[acetyl-CoA carboxylase 1]
AMP + diphosphate + acetyl-CoA carboxylase 1
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cytoplasmic acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotin carboxyl carrier protein
-
i.e. BCCP, substrate is the recombinantly expressed His-tagged biotinoyl domain, BCCP87, of Escherichia coli BCCP, binding pattern, overview
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-
?
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
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-
-
-
?
ATP + biotin + C-terminal domain of apo-biotin carboxyl carrier protein
AMP + diphosphate + biotinylated C-terminal domain of acetyl CoA carboxylase
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Escherichia coli BPL biotinylates both the homologous BCCP domain BCCP87 and the corresponding domain from Mycobacterium tuberculosis
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-
?
ATP + biotin + C-terminal domain of apo-biotin carboxyl carrier protein
AMP + diphosphate + biotinylated C-terminal domain of apo-biotin carboxyl carrier protein
Mycobacterium tuberculosis BPL specifically biotinylates the homologous BCCP domain BCCP87, but not the Escherichia coli domain BCCP87
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-
?
ATP + biotin + carboxyl carrier protein
?
-
the biotinylated product, holo biotin carboxyl carrier protein, forms a stable complex with the enzyme, which barely dissociates at room temperature
-
-
?
ATP + biotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + biotinylated CGGGSGGGSGLNDIFEAQKIEWH
-
-
-
-
?
ATP + biotin + chimeric protein of glutathione S-transferase and green fluorescence protein with biotin carboxyl carrier proteinDelta100
?
-
-
-
-
?
ATP + biotin + fluorescein-labeled peptide 85-11
ADP + diphosphate + biotinyl-fluorescein-labeled peptide 85-11
-
peptide 85-11 has the sequence MAGGLNDIFEAQKIEWHE with the lysine residue being targeted for biotinylation, development of a fluorescence polarization technology-based assay method, overview
-
-
?
ATP + biotin + GLNDIFEAQKIEWH
AMP + diphosphate + biotinylated GLNDIFEAQKIEWH
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i.e. Schatz' peptide, synthetic biotinable minimal peptide
-
-
?
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine
AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
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ATP in form of MgATP2-
-
-
?
ATP + biotin + [Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
AMP + diphosphate + [Escherichia coli biotin-carboxyl-carrier-protein mutant M136S]-biotinyl-L-lysine
-
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. Biotin carboxyl carrier protein becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
ATP + biotin + [Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
AMP + diphosphate + [Escherichia coli biotin-carboxyl-carrier-protein]-biotinyl-L-lysine
-
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. Biotin carboxyl carrier protein becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
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-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
ATP + cis-propargyl biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + cis-propargyl bioti-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + cis-propargyl biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + cis-propargyl biotin-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + desthiobiotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + desthiobiotinylated CGGGSGGGSGLNDIFEAQKIEWH
-
-
-
-
?
ATP + desthiobiotin azide + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + desthiobiotin azide-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
avitagged BirA + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
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recombinant Saccharomyces cerevisiae cells
-
-
?
avitagged BirA + biotin + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
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the recombinant avitagged enzyme biotinylates itself at the avitag sequence
-
-
?
biotin + ATP
biotinyl-5'-AMP + diphosphate
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first half-reaction of BPL
-
-
?
biotin + ATP + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
catalyzes the covalent attachment of the biotin prosthetic group to a specific lysine of the biotin carboxyl carrier domain of biotin-dependent carboxylases in a two-step reaction
-
r
D-biotin + ATP
biotinyl-5'-AMP + diphosphate
-
first half-reaction of BPL
-
-
?
ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
AccB, i.e. acetyl-CoA carboxylase biotin carboxyl carrier protein biotin attachment domain
-
-
?
ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
AccB, i.e. acetyl-CoA carboxylase biotin carboxyl carrier protein biotin attachment domain
-
-
?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
mitochondrial acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
i.e. ACC2, substrate is the recombinantly expressed His-tagged biotinoyl domain, ACC75, of ACC2, comprising residues 891-965. hHCS recognizes the MKM motif, NMR binding study, binding pattern, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
i.e. ACC2, substrate is the recombinantly expressed His-tagged biotinoyl domain, ACC75, of ACC2. The apo-biotinoyl domain is biotinylated at Lys929 to form the holoprotein
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
biotin binding structure with importance of arginine 40 in the glycine-rich motif in the specificity of the biotinylation reaction. The Arg40 residue from the conserved GXGRXG motif interacts with the carboxyl group of biotin and stabilizes the alpha- and beta-phosphates of the nucleotide, overview. Presence of biotin is not required for ATP binding to the wild-type enzyme in the absence of Mg2+, the binding of biotin and ATP occurs via a random but cooperative process
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of acetyl-CoA carboxylase, ACC
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of the pyruvate carboxylase, PC, of the organism, substrate is peptide fragment CaPC115 as GST-tagged recombinant protein, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of acetyl-CoA carboxylase, ACC
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
determination of the biotin domains of the pyruvate carboxylase, PC, of the organism, substrate is peptide fragment CaPC115 as GST-tagged recombinant protein, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotin protein ligase, BPL required to complete acetyl-CoA carboxylase's capability for fatty acid biosynthesis
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
the holo-enzyme is a multienzyme complex, in which biotin is bound to the biotin carboxyl carrier protein, binding structure, overview. All biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
conformational changes occur upon biotin binding. Structure-function relationship, modelling, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
incorporation of biotin into apo-carboxyl carrier protein, a subunit of acetyl-CoA carboxylase from E. coli
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
activation by biotinylation, HCS is the enzyme responsible for specifically attaching biotin onto the mammalian biotin domains. Biotinylation is catalysed through a two-step reaction where biotin is first activated to biotinyl-5'-AMP in an ATP-dependent manner, the biotin is then transferred onto the epsilon-amino group of a specific target lysine residue. All biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
activation by biotinylation. The biotinylated lysine itself is located in a hairpin turn between beta-strands 4 and 5 in the centre of the polypeptide, present in a Met-Lys-Met motif that is essentially invariant in all biotin domains. HCS may well contain proofreading activity to select appropriate substrates
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinylation site determination, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinylation site determination, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
overall reaction
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
overall reaction, BPL catalyses transfer of biotin to an epsilon-amino group of a specific lysine residue, which is usually the 35th amino acid from C-terminal of apoBCCP and converts it to active holoBCCP which promotes fatty acid initiation and elongation
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
structure-function relationship, modelling, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
structure-function relationship, modelling, overview
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
all biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
-
-
-
?
ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
-
-
-
?
ATP + biotin + Avi-tagged thioredoxin
?
-
biotin ligase site-specifically biotinylates a lysine side chain within a 15-amino acid acceptor peptide (also known as Avi-tag)
-
-
?
ATP + biotin + Avi-tagged thioredoxin
?
-
biotin ligase site-specifically biotinylates a lysine side chain within a 15-amino acid acceptor peptide (also known as Avi-tag)
-
-
?
ATP + biotin + BLAP
AMP + diphosphate + biotinylated BLAP
BLAP, i.e. biotin/lipoyl attachment protein
-
-
?
ATP + biotin + BLAP
AMP + diphosphate + biotinylated BLAP
BLAP, i.e. biotin/lipoyl attachment protein
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
-
-
-
-
?
ATP + biotin + PyC-77
AMP + diphosphate + biotinylated PyC-77
Pyc-77, i.e. pyruvate carboxylase biotin attachment domain
-
-
?
ATP + biotin + PyC-77
AMP + diphosphate + biotinylated PyC-77
Pyc-77, i.e. pyruvate carboxylase biotin attachment domain
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein mutant S136M]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
-
-
?
ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Sulfolobus tokodaii is unique in that its biotin carboxyl carrier protein has serine replaced for the methionine C-terminal to the lysine. This biotin carboxyl carrier protein is biotinylated by its own biotin protein ligase, but not by Escherichia coli biotin protein ligase. Likewise, Escherichia coli biotin carboxyl carrier protein is not biotinylated by Sulfolobus tokodaii biotin protein ligase
-
-
?
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
-
recombinant avitag-tagged maltose-binding protein
-
-
?
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
-
second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, BCCP, EC 6.3.4.14
-
-
?
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
-
second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, EC 6.3.4.14
-
-
?
additional information
?
-
-
evidence for a direct role of the biotin-[acetyl-CoA-carboxylase] ligase in repression of the biotin operon in Escherichia coli
-
-
?
additional information
?
-
-
also functions to repress the biotin biosynthetic operon and synthesizes its own corepressor, biotinyl-5'-AMP, the catalytic intermediate of the biotinylation reaction, catalyzes key reactions in essential metabolic processes, essential for survival
-
?
additional information
?
-
-
substrate specificities of wild-type enzyme and of mutant R118G, the first biotinylates only a single protein substrate, while the mutant shows a wider substrate spectrum
-
-
?
additional information
?
-
-
the enzyme site-specifically biotinylates proteins via a biotin acceptor peptide tag
-
-
?
additional information
?
-
-
does not use yeast acceptor peptide as a substrate
-
-
?
additional information
?
-
-
mammalian cell surface proteins tagged with a 15-amino acid peptide, i.e. the AP-tag, are specifically biotinylated by Escherichia coli biotin ligase BirA, whereas endogenous proteins are not modified, overview. BirA labels the AP-tag specifically in different cellular compartments: at the cell surface, in the endoplasmic reticulum, in the cytosol, and in the nucleus. BirA labeling may also be used in living animals, for example in a transgenic mouse expressing cytosolic BirA, overview
-
-
?
additional information
?
-
-
Escherichia coli enzyme undergoes self-biotinylation
-
-
?
additional information
?
-
-
acetyl-CoA carboxylase-1 and -2 perform the essential role of converting acetyl CoA to malonyl CoA, the first committed step in fatty acid synthesis, required for membrane biogenesis. The enzyme exists either as catalytic homodimers or associated with more highly active filamentous fibres. Development of an assay method using apo-pyruvate carboxylase partially purified from the livers of biotin-deficient rats for detection of biotin in fibroblast samples from healthy persons and patients with multiple carboxylase deficiency
-
-
?
additional information
?
-
-
protein-protein interaction between BPL and biotin-dependent enzymes is highly conserved. substrate recognition by BPLs occurs through conserved structural cues that govern the specificity of biotinylation, molecular modelling, overview. The region between Leu166 and Arg290 of BPL is required for catalysis. Development of an assay method using apo-pyruvate carboxylase partially purified from the livers of biotin-deficient rats for detection of biotin in samples from healthy persons and patients with multiple carboxylase deficiency
-
-
?
additional information
?
-
-
although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
the 4'-hydroxyazobenzene-2-carboxylic acid dye assay can be used to quantify biotin
-
-
?
additional information
?
-
-
the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain
-
-
?
additional information
?
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
additional information
?
-
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
additional information
?
-
enzyme is not able to biotinylate Schatz' minimal peptide GLNDIFEAQKIEWH
-
-
?
additional information
?
-
-
structural features influencing the reaction mechanism, overview
-
-
?
additional information
?
-
-
structural features influencing the reaction mechanism, overview
-
-
?
additional information
?
-
-
biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase
-
-
?
additional information
?
-
-
biotin protein ligase is a bifunctional protein, possessing both biotin ligase and transcription repressor activities
-
-
?
additional information
?
-
-
biotin protein ligase is a bifunctional protein, possessing both biotin ligase and transcription repressor activities
-
-
?
additional information
?
-
-
SH2 domain-based tyrosine kinase assay using biotin ligase modified with a terbium(III) complex. An SH2 domain from lymphocyte-specific tyrosine kinase is genetically fused to a truncated biotin carboxyl carrier protein, and the resulting fusion protein is labeled through biotinylation with biotin protein ligase carrying multiple copies of a luminescent Tb3+ complex. The labeled SH2 fusion proteins are employed to detect a phosphorylated peptide immobilized on the surface of the microtiter plate, where the phosphorylated peptide is produced by phosphorylation to the substrate peptide by Src tyrosine kinase. The assay allows for a reliable determination of the activity of Src kinase lower than 10 ng/mL
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-[acetyl-CoA carboxylase 1]
AMP + diphosphate + acetyl-CoA carboxylase 1
-
cytoplasmic acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
-
mitochondrial acetyl-CoA carboxylase isozyme
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
avitagged BirA + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
-
recombinant Saccharomyces cerevisiae cells
-
-
?
biotin + ATP
biotinyl-5'-AMP + diphosphate
-
first half-reaction of BPL
-
-
?
biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
-
second half-reaction of BPL, the apocarboxylase is the biotin-carboxyl-carrier protein, which is carboxylated after biotin binding by the biotin carboxylase, BCCP, EC 6.3.4.14
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
?
ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
biotin protein ligase, BPL required to complete acetyl-CoA carboxylase's capability for fatty acid biosynthesis
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
the holo-enzyme is a multienzyme complex, in which biotin is bound to the biotin carboxyl carrier protein, binding structure, overview. All biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
activation by biotinylation, HCS is the enzyme responsible for specifically attaching biotin onto the mammalian biotin domains. Biotinylation is catalysed through a two-step reaction where biotin is first activated to biotinyl-5'-AMP in an ATP-dependent manner, the biotin is then transferred onto the epsilon-amino group of a specific target lysine residue. All biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
overall reaction, BPL catalyses transfer of biotin to an epsilon-amino group of a specific lysine residue, which is usually the 35th amino acid from C-terminal of apoBCCP and converts it to active holoBCCP which promotes fatty acid initiation and elongation
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
all biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
additional information
?
-
-
evidence for a direct role of the biotin-[acetyl-CoA-carboxylase] ligase in repression of the biotin operon in Escherichia coli
-
-
?
additional information
?
-
-
also functions to repress the biotin biosynthetic operon and synthesizes its own corepressor, biotinyl-5'-AMP, the catalytic intermediate of the biotinylation reaction, catalyzes key reactions in essential metabolic processes, essential for survival
-
?
additional information
?
-
-
acetyl-CoA carboxylase-1 and -2 perform the essential role of converting acetyl CoA to malonyl CoA, the first committed step in fatty acid synthesis, required for membrane biogenesis. The enzyme exists either as catalytic homodimers or associated with more highly active filamentous fibres. Development of an assay method using apo-pyruvate carboxylase partially purified from the livers of biotin-deficient rats for detection of biotin in fibroblast samples from healthy persons and patients with multiple carboxylase deficiency
-
-
?
additional information
?
-
-
although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
additional information
?
-
-
biotin-dependent acetyl-CoA carboxylases/transcarboxylases are a class of enzymes that, in addition to fatty-acid biosynthesis, are important for gluconeogenesis as well as propionate catabolism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
binding structure, the solvent-exposed beta- and gamma-phosphates of ATP are located in the intersubunit cavity formed by the N- and C-terminal domains, the Arg40 residue from the conserved GXGRXG motif interacts with the carboxyl group of biotin and stabilizes the alpha- and beta-phosphates of the nucleotide, overview
biotin
-
dependent on, association of biotin and BPL is stabilized by 52 interactions, overview
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, cis-propargyl biotin, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues desthiobiotin azide, trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
additional information
-
no activity with biotin analogues trans-propargyl biotin, iminobiotin, diaminobiotin, nitrobenzoxadiazole gamma-butyric acid, iodouracil valeric acid, thiouracil valeric acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
the final step of the mechanism, the formation of biotinyl-5'-AMP, is Mg2+-dependent
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2'R,6'S)-9-[6'-([[N-(D-biotinoyl)sulfamoyl]oxy]methyl)morpholin-2'-yl]adenine
nucleoside-based inhibitor, KD value 0.324 nM
(3aS,4S,6aR)-4-(5-[1-[3-(naphthalen-2-yloxy)propyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-(5-[1-[4-(naphthalen-1-yloxy)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-(5-[1-[4-(naphthalen-2-yloxy)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-[-[1-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6ahexahydrothieno[3,4-d]imidazol-2-one
-
competitive inhibitor
(3aS,4S,6aR)-4-[4-[1-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]butyl]-1,3,3a,4,6,6a-hexa hydrothieno[3,4-d]imidazol-2-one
-
-
(3aS,4S,6aR)-4-[5-[1-(4-phenoxybutyl)-1H-1,2,3-triazol-4-yl]pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
-
(3aS,4S,6aR)-4-[5-[1-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6a-hexa hydrothieno[3,4-d]imidazol-2-one
-
-
(3aS,4S,6aR)-4-[5-[3-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-2-one
-
-
(3aS,4S,6aR)-4-[6-[1-[[(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2,2-dimethyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3]dioxol-6-yl]methyl]triazol-4-yl]hexyl]-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-2-one
-
-
2'-amino-5'-[N-(D-biotinoyl)sulfamoyl]amino-3',5'-dideoxyadenosine
nucleoside-based inhibitor, KD value 0.627 nM
2-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)ethyl 2,2-dimethylpropanoate
-
-
3-(2-oxo-1,3-benzoxazol-3(2H)-yl)-N-phenylpropanamide
-
inhibitor identified by molecular docking, glide score -7.49, glide energy -40.64 kcal/mol
5-chloro-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
not inhibitory to human enzyme at 0.08 mM
5-methyl-3-[3-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)propyl]-1,3-benzoxazol-2(3H)-one
-
-
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
9-[2'-azido-5'-O-[N-(D-biotinoyl)sulfamoyl]-2'-deoxy-beta-D-arabinofuranosyl]adenine
nucleoside-based inhibitor, KD value 0.027 nM. Strongest binding inhibitor in series
biotin acetylene
-
i.e. (3aS,4S,6aR)-4-hept-6-ynyl-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-2-one
GLNDIFEAQKIEWH
-
i.e. Schatz' peptide, synthetic biotinable minimal peptide, competitively inhibits self-biotinylation
N-(2-methylphenyl)-2-(2-oxo-1,3-benzoxazol-3(2H)-yl)acetamide
-
inhibitor identified by molecular docking, glide score -7.34, glide energy -37.68 kcal/mol
NaCl
-
inhibits the purified enzyme at 0.1 M, but not the immobilized enzyme in crude extract of recombinant yeast cells
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
competitive inhibitor versus biotin
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
not inhibitory to human enzyme at 0.08 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Exploring a Tumor-Intrinsic PD-L1 Signal with Proximity-Dependent Biotin Identification in Lung Cancer Cells.
Dengue
Expression, purification and characterization of in vivo biotinylated dengue virus envelope domain III based tetravalent antigen.
Infections
A new method to determine in vivo interactomes reveals binding of the Legionella pneumophila effector PieE to multiple rab GTPases.
Infections
Development of a novel bacteriophage based biomagnetic separation method as an aid for sensitive detection of viable Escherichia coli.
Infections
Simultaneous protein expression and modification: an efficient approach for production of unphosphorylated and biotinylated receptor tyrosine kinases by triple infection in the baculovirus expression system.
Infections
The root-invading pathogen Fusarium oxysporum targets pattern-triggered immunity using both cytoplasmic and apoplastic effectors.
Lipoma
Biotin ligase tagging identifies proteins proximal to E-cadherin, including lipoma preferred partner, a regulator of epithelial cell-cell and cell-substrate adhesion.
Tuberculosis
Crystallization and preliminary X-ray diffraction analysis of biotin acetyl-CoA carboxylase ligase (BirA) from Mycobacterium tuberculosis.
Tuberculosis
Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosis.
Tuberculosis
Mycobacterium smegmatis?BioQ defines a new regulatory network for biotin metabolism.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0052
apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
pH 8.0, 37°C
0.12
[Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.011
[Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.03 - 0.101
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
-
0.26
biotin
-
reaction with ATP + apo-carboxyl carrier protein, a subunit of acetyl-CoA carboxylase from E. coli
0.03
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 37°C, wild type enzyme
-
0.063
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 70°C, mutant enzyme A43G
-
0.101
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 70°C, wild type enzyme
-
0.00044
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, wild type enzyme
-
0.00058
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, mutant enzyme A43G
-
0.00058
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, wild type enzyme
-
additional information
additional information
isothermal titration calorimetry measurements of wild-type an dR40G mutant BPL with biotin and ATP, ATP and biotin binding are enthalpydriven with a favourable entropy change, overview
-
additional information
additional information
-
isothermal titration calorimetry measurements of wild-type an dR40G mutant BPL with biotin and ATP, ATP and biotin binding are enthalpydriven with a favourable entropy change, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.58
[Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.165
[Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.0097 - 0.165
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
-
0.8
biotin
-
mutant K321E, wild-type BCCP biotin domain and mutant K283E, E147Kmutant BCCP biotin domain
0.0097
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 37°C, wild type enzyme
-
0.082
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 70°C, mutant enzyme A43G
-
0.165
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 70°C, wild type enzyme
-
0.0022
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, mutant enzyme A43G
-
0.004
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, wild type enzyme
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
[Escherichia coli apo-biotin-carboxyl-carrier-protein mutant M136S]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
15
[Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
-
pH 8.0, 37°C, wild type enzyme
-
0.32 - 1.6
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
-
0.32
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 37°C, wild type enzyme
-
1.3
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 70°C, mutant enzyme A43G
-
1.6
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein mutant S136M]-lysine
pH 8.0, 70°C, wild type enzyme
-
3.8
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, mutant enzyme A43G
-
6.9
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C, wild type enzyme
-
9.1
[Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
pH 8.0, 70°C,wild type enzyme
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(3aS,4S,6aR)-4-(5-[1-[3-(naphthalen-2-yloxy)propyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
Ki above 0.01 mM, wild type enzyme, at pH 7.5 and 37°C
0.01
(3aS,4S,6aR)-4-(5-[1-[4-(naphthalen-1-yloxy)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
Ki above 0.01 mM, wild type enzyme, at pH 7.5 and 37°C
0.0017
(3aS,4S,6aR)-4-(5-[1-[4-(naphthalen-2-yloxy)butyl]-1H-1,2,3-triazol-4-yl]pentyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
wild type enzyme, at pH 7.5 and 37°C
0.00117
(3aS,4S,6aR)-4-[-[1-[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl]triazol-4-yl]pentyl]-1,3,3a,4,6,6ahexahydrothieno[3,4-d]imidazol-2-one
-
wild type enzyme, at pH 7.5 and 37°C
0.01
(3aS,4S,6aR)-4-[5-[1-(4-phenoxybutyl)-1H-1,2,3-triazol-4-yl]pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one
-
Ki above 0.01 mM, wild type enzyme, at pH 7.5 and 37°C
0.01
2-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)ethyl 2,2-dimethylpropanoate
-
Ki above 0.01 mM, wild type enzyme, at pH 7.5 and 37°C
0.01
5-methyl-3-[3-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)propyl]-1,3-benzoxazol-2(3H)-one
-
Ki above 0.01 mM, wild type enzyme, at pH 7.5 and 37°C
0.00009
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
-
wild type enzyme, at pH 7.5 and 37°C
0.0003
biotin acetylene
-
wild type enzyme, pH and temperature not specified in the publication
0.0072
biotin acetylene
-
mutant enzyme F123G, pH and temperature not specified in the publication
0.0076
biotin acetylene
-
mutant enzyme F123R, pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0006
5-chloro-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00009
5-methyl-3-[4-(4-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl]-1H-1,2,3-triazol-1-yl)butyl]-1,3-benzoxazol-2(3H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the immobilized enzyme is slightly less active than the soluble enzyme
additional information
biotin binding shows an equilibrium constant of 200 nMat 20°C. The equilibrium dissociation constant increases by approximately four fold on increasing the temperature from 10°C to 50°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
36
-
wild type enzyme and mutant enzymes birA311, birA825, birA301, and birA352
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
holocarboxylase synthetase catalyzes the biotinylation of the four biotin-dependent carboxylases found in human, mitochondrial propionyl-CoA carboxylase, pyruvate carboxylase, beta-methylcrotonyl-CoA carboxylase, and cytosolic acetyl-CoA carboxylase
-
-
brenda
enzyme detected in wild type Saccharomaces cerevisiae not in a mutant defective in biotin-[acetyl-CoA-carboxylase] ligase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
lung fibroblasts, quantitative determination of HCS in wild-type IMR-90 fibroblasts and in those recombinantly overexpressing human telomerase, evaluation as a cell model for investigation of HCS in epigenetic regulation, histone biotinylation in aging cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
isozyme subcellular localization, immunofluorescence study, overview
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
biotin deficiency, e.g. occuring in patients with BTD deficiency, in severely malnourished children in developing countries, and in individuals consuming large amounts of raw egg white which contains the protein avidin, has adverse effects on cellular and humoral immune functions, and it can lead to candida dermatitis and presented with absent delayed-hypersensitivity skin-tests responses, IgA deficiency, and subnormal percentages of T-lymphocytes in peripheral blood, overview
malfunction
-
deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes
malfunction
-
holocarboxylase synthetase, HCS, deficiency is an inborn error of biotin metabolism, leading to a multiple carboxylases deficiency. A Japanese male neonate with HCS deficiency received maternal administration of biotin from 33 weeks gestation, acylcarnitine profiles compared to control, phenotype, overview
metabolism
-
holocarboxylase synthetase governs the cellular fate of the essential micronutrient biotin, i.e. vitamin H or B7
metabolism
-
holo-BPL is protected from proteolysis by biotinyl-5'-AMP, an intermediate of the BPL-catalyzed reaction. Apo-MtBPL is completely digested by trypsin within 20 min of co-ncubation. Substrate selectivity and inability to promote self biotinylation are exquisite features of Mycobacterium tuberculosis BPL
metabolism
holo-BPL is protected from proteolysis by biotinyl-5'-AMP, an intermediate of the BPL-catalyzed reaction. Apo-MtBPL is completely digested by trypsin within 20 min of co-ncubation. Substrate selectivity and inability to promote self biotinylation are exquisite features of Mycobacterium tuberculosis BPL
physiological function
-
HCS is responsible for attaching biotin onto the biotin-dependent enzymes that reside in the cytoplasm and mitochondria
physiological function
-
holocarboxylase synthetase 1 physically interacts with histone H3 in Arabidopsis
physiological function
BirA is an effective regulator of biotin operon transcription. Deletion of the DNA binding domain of BirA results in loss of virtually all of its ligation activity
physiological function
BirA regulates transcription at three genomic sites: bioWAFDBI, yuiG and yhfUTS. The N-terminal DNA binding domain can be deleted from Bacillus subtilis BirA without adverse effects on its ligase function
physiological function
-
expression of biotin operon genes bioW, bioA, bioF, bioD, bioB, and bioI in Corynebacterium glutamicum. The recombinant strain is able to produce lysine in a medium lacking biotin, and the lysine yield on glucose is similar to what is obtained when using a medium containing biotin. Specific growth rate decreases by of 20% when the strain is cultivated without biotin. Neither pyruvate carboxylase pycA nor biotin ligase birA overexpression, whether alone or in combination, has an effect on specific growth rate
physiological function
-
Francisella novicida encodes two biotin protein ligases. BirA and BplA are both functional biotin protein ligases. BirA has a ligase domain as well as an N-terminal DNA-binding regulatory domain. BirA, but not BplA, regulates transcription of the biotin synthetic operon, regulating and thereby likely preventing wasteful synthesis of biotin. Isoform BplA lacks the N-terminal DNA binding motif and is more efficient in ligase reaction than BirA. Expression of BplA (but not birA) increases significantly during infection of macrophages. BplA (but not BirA) is required for bacterial replication within macrophages as well as in mice
physiological function
-
expression of biotin operon genes bioW, bioA, bioF, bioD, bioB, and bioI in Corynebacterium glutamicum. The recombinant strain is able to produce lysine in a medium lacking biotin, and the lysine yield on glucose is similar to what is obtained when using a medium containing biotin. Specific growth rate decreases by of 20% when the strain is cultivated without biotin. Neither pyruvate carboxylase pycA nor biotin ligase birA overexpression, whether alone or in combination, has an effect on specific growth rate
-
physiological function
-
BirA regulates transcription at three genomic sites: bioWAFDBI, yuiG and yhfUTS. The N-terminal DNA binding domain can be deleted from Bacillus subtilis BirA without adverse effects on its ligase function
-
physiological function
-
BirA is an effective regulator of biotin operon transcription. Deletion of the DNA binding domain of BirA results in loss of virtually all of its ligation activity
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
2 * 26000, calculated. Equilibrium analytical ultracentrifugation measurements performed on the apoenzyme and its complexes with biotin and bio-5-AMP all yield molecular weights for the protein consistent with a dimer. Regardless of ligation state the Pyrococcus horikoshii enzyme is a dimer
26071
-
2 * 26071 recombinant enzyme, SDS-PAGE and amino acid sequence calculation
7909
-
liquid-chromatography electrospray ionisation ion-trap mass spectroscopy
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
-
2 * 26071 recombinant enzyme, SDS-PAGE and amino acid sequence calculation
dimer
-
the functional unit is a dimer, a subunit contains a catalytic N-terminal domain and a C-terminal domain, structure analysis
dimer
-
the protein is a constitutive dimer, i.e. dimerises independently of biotin binding
dimer
2 * 26000, calculated. Equilibrium analytical ultracentrifugation measurements performed on the apoenzyme and its complexes with biotin and bio-5'-AMP all yield molecular weights for the protein consistent with a dimer. Regardless of ligation state the Pyrococcus horikoshii enzyme is a dimer
dimer
-
2 * 26071 recombinant enzyme, SDS-PAGE and amino acid sequence calculation
-
dimer
-
the functional unit is a dimer, a subunit contains a catalytic N-terminal domain and a C-terminal domain, structure analysis
-
dimer
-
the protein is a constitutive dimer, i.e. dimerises independently of biotin binding
-
additional information
ligand-free structure, and biotin-ATP intermediate complex of the enzyme, comparison of wild-type and mutant structures, overview
additional information
-
ligand-free structure, and biotin-ATP intermediate complex of the enzyme, comparison of wild-type and mutant structures, overview
additional information
EcBPL contains three distinct domains determined through X-ray crystallography. Monomeric and dimeric forms of the enzyme are involved in enzyme regulation, overview. Structure-function relationship, overview. EcBPL contains a DNA binding motif
additional information
-
structure-activity molecular modelling. Acetyl-CoA carboxylase-1 exists either as catalytic homodimers or associated with more highly active filamentous fibres. The region between Leu166 and Arg290 is required for catalysis
additional information
-
the N-terminal domain has a crucial effect on the enzymatic activity. The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS. It recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain. Human HCS shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus
additional information
-
BPL forms a weak dimer with bio-5'-AMP synthesized from ATP and biotin, on catalysis BPL forms monomeric and a weakly formed physiological dimer, both of which are holoenzymes
additional information
-
acetyl-CoA carboxylase biotinyl domain structure analysis, overview
additional information
-
acetyl-CoA carboxylase biotinyl domain structure analysis, overview
-
additional information
biotin-protein-ligase/holo-biotin-carboxyl-carrier-protein complex
additional information
-
biotin-protein-ligase/holo-biotin-carboxyl-carrier-protein complex
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant R40G enzymes free and in complex with ligands ATP and/or biotin, hanging drop vapour diffusion method, 0.002 ml of protein solution with 5 or 6 mg/ml wild-type or mutant protein, respectively, is mixed with 0.001 ml of reservoir solution containing 0.1M Mes, 0.2 M ammonium sulfate, 15% w/v PEG 5000 monoethyl ether, pH 6.5, with or without 2 mM D-biotin and 5 mM ATP, 17°C, a few hours for the free enzyme, 4-14 days for the complexed enzyme, X-ray diffraction structure determination and analysis at 2.3-2.55 A resolution, molecular modeling
EcBPL domains determination through X-ray crystallography at 2.3 A resolution, and determination of the crystal structure of EcBPL in complex with biotin
purified recombinant enzyme, 0.003 ml of 5 mg/ml protein in 2.5 mM desthiobiotin in 20 mM Tris-HCl pH 8.0, 50 mM NaCl, 1 mM PMSF and 1 mM DTT, is mixed with 0.003 ml of reservoir solution containing 12-16% w/v of both PEG 4000 and PEG 8000 in 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.8 A resolution
structures of dehydrated and hydrated BirA, at 2.69 A and 2.8 A resolution, respectively. Dehydration of BirA crystals traps both the apo and active conformations in its asymmetric unit. The crystal lattice rearrangement due to shrinkage in the dehydrated Mtb-BirA crystals ensues structural order of otherwise flexible ligand-binding loops L4 and L8 in apo BirA. In addition, crystal dehydration results in a shift of 3.5 A in the flexible loop L6, a proline-rich loop unique to Mycobacterium tuberculosis complex as well as around the L11 region. The shift in loop L11 in the C-terminal domain on dehydration emulates the action responsible for the complex formation with its protein ligand biotin carboxyl carrier protein domain of ACCA3. The two subunits A and B, though related by a noncrystallographic twofold symmetry, assemble into an asymmetric dimer representing the ligand-bound and ligand-free states of the protein, respectively
structures of the apo-form and in complex with reaction intermediate biotinyl-5'-AMP. Binding of the reaction intermediate leads to clear disorder-to-order transitions. A conserved lysine, Lys138, in the active site is essential for biotinylation
PhBPL in complex with biotin, ATP and biotinyl-5'-AMP, X-ray diffraction and structure analysis at 1.6 A, 1.6 A, 1.45 A resolution, respectively. Structure-function relationship, modelling, overview
-
purified recombinant enzyme, complexed with biotinyl-5'-AMP, biotin, adenosine, or mutant biotin carboxyl carrier protein PhBCCPN76, X-ray diffraction structure determination at 2.0-2.7 A resolution, analysis, and modelling. The non-hydrolyzable intermediate analogue biotinol-5'-AMP does not provide analyzable complex crystals
-
purified recombinant native and selenomethionine-labeled enzyme comprising residues 1-125, sitting drop method, 9.87 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 500 mM NaCl, 0.001 ml protein solution is mixed with 0.001 ml precipitation solution containing 10.5% PEG 2000, 0.1 M acetate-NaOH, pH 5.5, the drop is overlaid with a 1:1 mixture of silicone and paraffin oil allowing slow water evaporation from the drop, 22°C, preliminary X-ray diffraction structure determination and analysis at 1.45-1.6 A resolution
-
purified recombinant native and selenomethionine-labeled enzyme, sitting drop method, 9.87 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 500 mM NaCl, 0.001 ml protein solution is mixed with 0.001 ml precipitation solution containing 10.5% PEG 2000, 0.1 M acetate-NaOH, pH 5.5, the drop is overlaid with a 1:1 mixture of silicone and paraffin oil allowing slow water evaporation from the drop, 22°C, preliminary X-ray diffraction structure determination and analysis at 1.45-1.6 A resolution
-
apoenzyme, in complex with biotin, and complexed with biotinyl-5'-AMP, hanging drop vapor diffusion method, using
-
hanging drop vapor diffusion method, using 8-12% (w/v) PEG8000 in 0.1 M Tris pH 7.5 or 8.0 and 10% (v/v) glycerol
-
molecular docking of benzoxazolone derivatives in the active site region. Presence of a functional group attached either to the benzene ring or to the pyrole ring incresases binding efficacy
-
purified recombinant enzyme, hanging-drop vapour-diffusion method, 0.001 ml of 15 mg/ml protein solution is mixed with 0.001 ml of reservoir solution containing 8% PEG 8000 and 0.1 M TrisHCl pH 8.0., at 4°C or 20°C, crystals appear within 24 h, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R40G
site-directed mutagenesis, the structure of the mutant enzyme in both the ligand-free and biotin-bound forms reveals that the mutated loop has collapsed, thus hindering ATP binding. The mutant is catalytically active but shows poor substrate specificity. The affinity for biotin is reduced 3.5fold by the R40G mutation, but binding of ATP to mutant R40G is very weak in the absence or in the presence of biotin. Comparison to the equivalent mutant of Escherichia coli BirA, overview
DELTA1-81
elimination of N-terminal domain plus part of the central domain, loss of ligase activity
DELTA2-63
elimination of N-terminal domain, mutant shows normal ligase activity
DELTA2-65
elimination of N-terminal domain, mutant shows normal ligase activity
DELTA1-81
-
elimination of N-terminal domain plus part of the central domain, loss of ligase activity
-
DELTA2-63
-
elimination of N-terminal domain, mutant shows normal ligase activity
-
DELTA2-65
-
elimination of N-terminal domain, mutant shows normal ligase activity
-
G115S
I11V/P85S/ M157T/K163E/I224T
-
17fold increase in the ability to use desthiobiotin as a substrate
L237P
the mutant shows reduced catalytic activity compared to the wild-type enzyme
Q41R/M157T/I224T/E215D/T225A
-
10fold increase in the ability to use desthiobiotin as a substrate
R118G
D571N
-
naturally occuring mutation, important in positioning K579 in the AMP binding site
D615Y
-
naturally occuring mutation in the loop between alpha3 and beta6 that cover AMP, may coordinate oxygens of the AMP phosphate
D634Y
-
naturally occuring mutation of a solvent exposed residue, distal to active site on alpha4 and alpha5, respectively
D715G
-
naturally occuring mutation on beta9, may be involved in capping and stabilising the catalytic domain structure
G518E
-
naturally occuring mutation close to the active site and part of the ligand-binding loop, the mutation may not allow as much flexibility of this loop. As part of the hydrophobic pocket, making this polar residue would perturb biotin binding
G581S
-
naturally occuring mutation of a residue involved in hydrophobic interactions with biotin in the binding pocket
G582R
-
naturally occuring mutation of a residue involved in hydrophobic interactions with biotin in the binding pocket
L470S
-
naturally occuring mutation in an unstructured loop distal to the ligand-binding site
R508W/N511K
-
naturally occuring mutation of a residue critical in loop covering the ligand-binding site. R508 co-ordinates to the backbone carbonyl N712 to form a salt bridge, removing this would result in a more flexible loop, analogous to EcBPL R118 and R121 that co-ordinate oxygens within the AMP phosphate group
T462I
-
naturally occuring mutation in an unstructured loop distal to the ligand-binding site
V547G
-
naturally occuring mutation of a buried hydrophobic residue in alpha2 that reside near the AMP-binding beta5 strand
V550M
-
naturally occuring mutation of a buried hydrophobic residue in alpha2 that reside near the AMP-binding beta5 strand
Y456C
-
naturally occuring mutation in an unstructured loop distal to the ligand-binding site
R69A
the binding constant for biotin is nearly the same as that observed for the wild type protein. Mutant does not undergo self-botinylation
R48A/K111A
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the double mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant. Interface charge distribution in the double mutant complex, overview
R48K
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant
R48A/K111A
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the double mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant. Interface charge distribution in the double mutant complex, overview
-
R48K
-
site-directed mutagenesis, comparison of the nucleotide binding mode in the mutant to that in the wild-type enzyme, the active site loop Gly45-Trp53 is disordered in the mutant
-
DELTA1-81
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
DELTA2-65
elimination of N-terminal domain, complete loss of ligase activity
DELTA2-74
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
F123G
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
F123R
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
R125A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R125N
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R125A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
R125N
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
F123G
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
-
F123R
-
the mutation has minimal effect upon the Km value for MgATP and biotin. In contrast, the kcat for biotin and MgATP are significantly compromised to about 10% that of wild type enzyme
-
DELTA1-81
-
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
-
DELTA2-65
-
elimination of N-terminal domain, complete loss of ligase activity
-
DELTA2-74
-
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity
-
A43G
additional information
G115S
-
site-directed mutagenesis, the mutant enzyme shows a highly increased rate of biotinyl-5'-AMP intermediate formation, but no release of the intermediate
R118G
-
site-directed mutagenesis, the mutant enzyme shows a wider substrate specificity compared to the wild-type enzyme, the mutant biotinylates bovine serum albumin, chloramphenicol acetyltransferase, immunoglobin heavy and light chains, and RNase A in vitro, it also self-biotinylates in vivo and in vitro, the activity depends on proximity, distance to the substrate can be bridged by a linker like avidin, overview
R118G
mutation of Arg118 to glycine in EcBPL causes altered affinity of BPL for biotin, increased dissociation rates for biotin and biotinyl-5'-AMP, and consequently, promiscuous biotinylation of inappropriate proteins
A43G
catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme
A43G
-
catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme
-
additional information
-
disruption of BPL affects important metabolic pathways such as fatty acid biosynthesis and gluconeogenesis
additional information
-
disruption of BPL affects important metabolic pathways such as fatty acid biosynthesis and gluconeogenesis
-
additional information
-
mammalian cell surface proteins tagged with a 15-amino acid peptide, i.e. the AP-tag, are specifically biotinylated by Escherichia coli biotin ligase BirA, whereas endogenous proteins are not modified, overview. BirA labels the AP-tag specifically in different cellular compartments: at the cell surface, in the endoplasmic reticulum, in the cytosol, and in the nucleus of mammalian cells, including human, mouse, rat and hamster cell lines, and primary neuron culture. BirA labeling may also be used in living animals, for example in a transgenic mouse expressing cytosolic BirA, overview. Benefit of streptavidin labeling over Ab labeling, method development, detailed overview
additional information
mutational analysis, overview. The C-terminal 87 amino acids of biotin carboxyl carrier protein, i.e. BCCP-87, are recognised and biotinylated by BPL as well as full-length BCCP due to the fact that this peptide adopts the tertiary structure that is required for the interaction with BPL
additional information
-
HCS mutants with deletions up to Ala235 or Thr266 still show catalytic activity and can complement an enzyme-deficient Escherichia coli birA- strain. Enzyme deficiency can cause symptoms like ketoacidosis, feeding difficulties, hypotonia, seizures, developmental delay and dermal abnormalities such as rashes, dryness of the skin and alopecia, multiple carboxylase deficiency is caused by a lack of activity of the biotin-dependent enzymes, phenotypes, overview. Molecular modelling of mutations causing HCS deficiency, detailed overview
additional information
-
construction of biotinylated magnetic nanoparticles, with or without introduced strepatavidin, by displaying biotin acceptor peptide or biotin carboxyl carrier protein, BCCP, on the surface of bacterial magnetic particles for analysis of in vitro biotinylation, method development and evaluation, overview
additional information
-
construction of biotinylated magnetic nanoparticles, with or without introduced strepatavidin, by displaying biotin acceptor peptide or biotin carboxyl carrier protein, BCCP, on the surface of bacterial magnetic particles for analysis of in vitro biotinylation, method development and evaluation, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
melting temperature, BirA-GFP fusion protein. Enzyme is not able to refold after the first cycle of heat denaturation
61
melting temperature, BirA-GFP fusion protein, presence of 1 mM biotin
71
melting temperature, BirA-GFP fusion protein, presence of both 1 mM biotin and 1 mM ATP
additional information
additional information
-
mutant enzymes birA707, birA361 and birA91 with strikingly altered thermosensitivity
additional information
melting temperature does not change significantly in presence of ATP, GTP, CTP or UTP
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 1-2 mg/ml purified recombinant His6-tagged enzyme, in 50 mM Tris-HCl, pH 7.5, 0.5 mM EDTA, pH 8.0, 250 mM NaCl, at least 6 months without loss of activity
-
4°C, immobilized recombinant enzyme, PBS, completely stable for 4 weeks, loss of activity after 5 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, Ni-NTA resin column chromatography, and Superdex 75 gel filtration
-
recombinant C-terminally Strep-tagged BirA from Escherichia coli
recombinant enzyme comprising residues 1-125 from Escherichia coli strain BL21
-
recombinant enzyme from Escherichia coli
recombinant enzyme from Escherichia coli strain BL21 in a chromatographic procedure comprising several steps
-
recombinant enzyme from Escherichia coli, the human enzyme degrades significantly during isolation
-
recombinant enzyme from Saccharomyces cerevisiae, immobilization of the recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
recombinant His-tagged wild-type and mutant enzymes from strain JM109 by nickel affinity chromatography
-
recombinant His6-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
-
recombinant His9-tagged BPL from Saccharomyces cerevisiae strain w303 by nickel affinity and cation exchange chromatography
-
recombinant human HCS from Hi5 insect cells by nickel affinity chromatography, anion exchange chromatography, and gel filtration
-
Super Q Toyopearl 650M column chromatography, Bio-Scale CHT-20-I column chromatography, and HiLoad 16/60 Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coding region of birA biotin-protein ligase gene cloned from genomic DNA by PCR, verfied by sequencing and expressed in mouse erythroleukemic cells
-
construction and expression of the C-terminal 87 amino acids of biotin carboxyl carrier protein, i.e. BCCP-87. cross-species activity of BPLs permitts functional cloning of the cDNA for yeast BPL through genetic complementation with a conditional lethal birA- strain of Escherichia coli
cross-species activity of BPLs permitts functional cloning of the cDNA for human BPL through genetic complementation with a conditional lethal birA? strain of Escherichia coli
-
cross-species activity of BPLs permitts functional cloning of the cDNA for yeast BPL through genetic complementation with a conditional lethal birA? strain of Escherichia coli
-
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21
-
doxycycline-regulated expression of a secreted variant of Escherichia coli biotin ligase BirA with target proteins containing a 13-residue biotin acceptor peptide appended to their extracellular domain, co-expression with three different G-protein coupled receptors, i.e. protease-activated receptors 1 and 2, and the platelet ADP receptor, P2Y12, which become biotinylated, in CHO-K1 Tet-On cells on the cell surface, overview
-
expressed as thioredoxin- and maltose binding protein-fusion proteins in Escherichia coli BL21(DE3) cells
-
expression of BirA from pET-based vector pHBA in Escherichia coli BL21 (lambdaDE3)
-
expression of HCS in Spodoptera frugiperda Sf9 cells and in Hi5 insect cells using the baculovirus transfection system
-
expression of His9-tagged BPL in Saccharomyces cerevisiae strain w303, functional complementation of the conditional lethal birA85 Escherichia coli strain BM4062
-
gene birA, expression of His-tagged wild-type and mutant enzymes in strain JM109, expression of enzyme in strain BM4092 unbiotinylated form
-
gene birA, functional expression of N-terminally and C-terminally multiply tagged enzyme in Saccharomyces cerevisiae, low level expression of the surface-displayed enzyme, expression of avitagged-BirA in Saccharomyces cerevisiae, overview
-
gene Rv3279c, DNA and amino acid sequence determination and analysis, expression of C-terminally Strep-tagged BirA in Escherichia coli
overexpression in Escherichia coli
overexpression of the enzyme comprising residues 1-125 in Escherichia coli strain BL21
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
-
BirA can be useful for specific in vivo labeling of proteins in cell cultures by biotinylation
drug development
synthesis
analysis
-
biotin-mediated ATP-diphosphate assay which does not require the isolation of the apoenzyme and is simple and convenient for use on a routine assay. The procedure is specifically designed for assay of enzyme from adipose tissue of biotin-deficient rats. W
analysis
-
biotinylation of apo-carboxyl carrier protein, a subunit of acetyl-CoA carboxylase from E. coli is a sensitive and convenient assay method for biotin-[acetyl-CoA-carboxylase] ligase
analysis
-
SH2 domain-based tyrosine kinase assay using biotin ligase modified with a terbium(III) complex. An SH2 domain from lymphocyte-specific tyrosine kinase is genetically fused to a truncated biotin carboxyl carrier protein, and the resulting fusion protein is labeled through biotinylation with biotin protein ligase carrying multiple copies of a luminescent Tb3+ complex. The labeled SH2 fusion proteins are employed to detect a phosphorylated peptide immobilized on the surface of the microtiter plate, where the phosphorylated peptide is produced by phosphorylation to the substrate peptide by Src tyrosine kinase. The assay allows for a reliable determination of the activity of Src kinase lower than 10 ng/mL
analysis
development of a high-throughput assay building on the principle of differential scanning fluorimetry of GFP-tagged proteins
analysis
-
fluorescent probe (4S)-4-[5-(1-[3-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]propyl]-1H-1,2,3-triazol-4-yl)pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one is synthesized by Bpl in vivo, accumulates in cytoplasm and can be used to gain insights into the mechanism of uptake, efflux and metabolism of BPL inhibitors
analysis
-
development of a high-throughput assay building on the principle of differential scanning fluorimetry of GFP-tagged proteins
-
drug development
-
the enzyme is a potential target for anti-mycobacterial drugs
drug development
-
the enzyme is a target for the design of effective antifungal drugs
drug development
the enzyme is a target for the design of effective antitubercular drugs
drug development
-
the enzyme is a target for the design of effective antifungal drugs
-
synthesis
-
the enzyme is utilized to synthesize site-specific biotinylated proteins via a biotin acceptor peptide tag
synthesis
-
in vivo biotinylation of bacterial magnetic particles synthesized by Magnetospirillum magneticum AMB-1 by heterologous expression of Escherichia coli biotin ligase. To biotinylate bacterial magnetic particles in vivo, biotin acceptor peptide is fused to a bacterial magnetic particles surface protein, Mms13, and Escherichia coli biotin ligase is simultaneously expressed in the truncated form lacking the DNA-binding domain. The biotinylated biotin acceptor protein-displaying bacterial magnetic particles are then exposed to streptavidin by simple mixing. The streptavidin-binding capacity of bacterial magnetic particles biotinylated in vivo is 35fold greater than that of bacterial magnetic particles biotinylated in vitro
synthesis
production of [35S]-biotin from Na-35SO4 and desthiobiotin with a specific activity of 30.7 Ci/mmol by expression of the biotinylation domain from the Plasmodium falciparum acetyl-CoA carboxylase in Escherichia coli as a biotinylation substrate. Overexpression of the biotin synthase, BioB, and biotin ligase, BirA, increases biotinylation of the biotinylation domain 160fold over basal levels. Biotinylated biotinylation domain is purified by affinity chromatography, and free biotin is liberated using acid hydrolysis
synthesis
site-directed antibody immobilization by fusing biotin carboxyl carrier protein BCCP to the IgG-binding domain of Protein A, and the resulting fusion protein is immobilized on the biotin protein ligase-modified gold surface of the sensor chip for quartz crystal microbalance through complexation between BCCP and biotin protein ligase. The layer of the IgG-binding domain is successfully captured the antibody, and the antibody retains high antigen-binding capability
synthesis
-
site-directed antibody immobilization by fusing biotin carboxyl carrier protein BCCP to the IgG-binding domain of Protein A, and the resulting fusion protein is immobilized on the biotin protein ligase-modified gold surface of the sensor chip for quartz crystal microbalance through complexation between BCCP and biotin protein ligase. The layer of the IgG-binding domain is successfully captured the antibody, and the antibody retains high antigen-binding capability
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dupuis, L.; Leon-del Rio, A.; Leclerc, D.; Campeau, E.; Sweetman, L.; Saudubray, J.M.; Herman, G.; Gibson, K.M.; Gravel, R.A.
Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency
Hum. Mol. Genet.
5
1011-1016
1996
Homo sapiens
brenda
Barker, D.F.; Campbell, A.M.
The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
J. Mol. Biol.
146
451-467
1981
Escherichia coli
brenda
Barker, D.F.; Campbell, A.M.
Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli
J. Mol. Biol.
146
469-492
1981
Escherichia coli
brenda
Mishina, M.; Roggenkamp, R.; Schweizer, E.
Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin:apocarboxylase ligase
Eur. J. Biochem.
111
79-87
1980
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Landman, A.D.; Desjardins, P.R.; Dakshinamurti, K.
A simple assay for acetyl-CoA holocarboxylase synthetase
Can. J. Biochem.
54
813-815
1976
Rattus norvegicus
brenda
Landman, A.D.; Dakshinamurti, K.
Enzymatic diagnosis of holocarboxylase synthetase deficiency using apo-carboxyl carrier protein as a substrate
Clin. Chim. Acta
251
41-52
1996
Homo sapiens
brenda
de Boer, E.; Rodriguez, P.; Bonte, E.; Krijgsveld, J.; Katsantoni, E.; Heck, A.; Grosveld, F.; Strouboulis, J.
Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice
Proc. Natl. Acad. Sci. USA
100
7480-7485
2003
Escherichia coli
brenda
Chapman-Smith, A.; Mulhern, T.D.; Whelan, F.; Cronan, J.E., Jr.; Wallace, J.C.
The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity
Protein Sci.
10
2608-2617
2001
Escherichia coli
brenda
Bagautdinov, B.; Kuroishi, C.; Sugahara, M.; Kunishima, N.
Purification, crystallization and preliminary crystallographic analysis of the biotin-protein ligase from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
61
193-195
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Parthasarathy, R.; Bajaj, J.; Boder, E.T.
An immobilized biotin ligase: surface display of Escherichia coli BirA on Saccharomyces cerevisiae
Biotechnol. Prog.
21
1627-1631
2005
Escherichia coli
brenda
Bagautdinov, B.; Kuroishi, C.; Sugahara, M.; Kunishima, N.
Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation
J. Mol. Biol.
353
322-333
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Choi-Rhee, E.; Schulman, H.; Cronan, J.E.
Promiscuous protein biotinylation by Escherichia coli biotin protein ligase
Protein Sci.
13
3043-3050
2004
Escherichia coli
brenda
Bagautdinov, B.; Matsuura, Y.; Bagautdinova, S.; Kunishima, N.
Crystallization and preliminary X-ray crystallographic studies of the biotin carboxyl carrier protein and biotin protein ligase complex from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
63
334-337
2007
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Sueda, S.; Li, Y.Q.; Kondo, H.; Kawarabayasi, Y.
Substrate specificity of archaeon Sulfolobus tokodaii biotin protein ligase
Biochem. Biophys. Res. Commun.
344
155-159
2006
Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii 7 (F9VNG7)
brenda
Streaker, E.D.; Beckett, D.
The biotin regulatory system: kinetic control of a transcriptional switch
Biochemistry
45
6417-6425
2006
Escherichia coli
brenda
Chen, I.; Choi, Y.A.; Ting, A.Y.
Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins
J. Am. Chem. Soc.
129
6619-6625
2007
Saccharomyces cerevisiae, Escherichia coli
brenda
Gralla, M.; Camporeale, G.; Zempleni, J.
Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus
J. Nutr. Biochem.
19
400-408
2008
Homo sapiens
brenda
Bennett, C.B.; Westmoreland, T.J.; Verrier, C.S.; Blanchette, C.A.; Sabin, T.L.; Phatnani, H.P.; Mishina, Y.V.; Huper, G.; Selim, A.L.; Madison, E.R.; Bailey, D.D.; Falae, A.I.; Galli, A.; Olson, J.A.; Greenleaf, A.L.; Marks, J.R.
Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction
PLoS ONE
3
e1448
2008
Mycobacterium tuberculosis
brenda
Gupta, V.; Gupta, R.K.; Khare, G.; Surolia, A.; Salunke, D.M.; Tyagi, A.K.
Crystallization and preliminary X-ray diffraction analysis of biotin acetyl-CoA carboxylase ligase (BirA) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
524-527
2008
Mycobacterium tuberculosis (P96884), Mycobacterium tuberculosis
brenda
Pendini, N.R.; Polyak, S.W.; Booker, G.W.; Wallace, J.C.; Wilce, M.C.
Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus
Acta Crystallogr. Sect. F
F64
520-523
2008
Staphylococcus aureus
brenda
Ng, B.; Polyak, S.W.; Bird, D.; Bailey, L.; Wallace, J.C.; Booker, G.W.
Escherichia coli biotin protein ligase: characterization and development of a high-throughput assay
Anal. Biochem.
376
131-136
2008
Escherichia coli
brenda
Maeda, Y.; Yoshino, T.; Takahashi, M.; Ginya, H.; Asahina, J.; Tajima, H.; Matsunaga, T.
Noncovalent immobilization of streptavidin on in vitro- and in vivo-biotinylated bacterial magnetic particles
Appl. Environ. Microbiol.
74
5139-5145
2008
Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1
brenda
Pendini, N.R.; Bailey, L.M.; Booker, G.W.; Wilce, M.C.; Wallace, J.C.; Polyak, S.W.
Biotin protein ligase from Candida albicans: expression, purification and development of a novel assay
Arch. Biochem. Biophys.
479
163-169
2008
Candida albicans, Candida albicans CBF562
brenda
Pendini, N.R.; Bailey, L.M.; Booker, G.W.; Wilce, M.C.; Wallace, J.C.; Polyak, S.W.
Microbial biotin protein ligases aid in understanding holocarboxylase synthetase deficiency
Biochim. Biophys. Acta
1784
973-982
2008
Saccharomyces cerevisiae, Homo sapiens, Pyrococcus horikoshii, Escherichia coli (P06709), Pyrococcus horikoshii OT-3
brenda
Slavoff, S.A.; Chen, I.; Choi, Y.; Ting, A.Y.
Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species
J. Am. Chem. Soc.
130
1160-1162
2008
Bacillus subtilis, Leuconostoc mesenteroides, Saccharomyces cerevisiae, Escherichia coli, Giardia intestinalis, Homo sapiens, Methanocaldococcus jannaschii, Cutibacterium acnes, Pyrococcus horikoshii, Trypanosoma cruzi
brenda
Bagautdinov, B.; Matsuura, Y.; Bagautdinova, S.; Kunishima, N.
Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate
J. Biol. Chem.
283
14739-14750
2008
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Howarth, M.; Ting, A.Y.
Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin
Nat. Protoc.
3
534-545
2008
Escherichia coli
brenda
Mize, G.J.; Harris, J.E.; Takayama, T.K.; Kulman, J.D.
Regulated expression of active biotinylated G-protein coupled receptors in mammalian cells
Protein Expr. Purif.
57
280-289
2008
Escherichia coli
brenda
Verhaegen, M.; Christopoulos, T.
Recombinant Gaussia luciferase: Overexpression, purification, and analytical application of a bioluminescent reporter for DNA hybridization
Anal. Chem.
74
4378-4385
2002
Escherichia coli K-12 (P06709)
brenda
Bailey, L.M.; Wallace, J.C.; Polyak, S.W.
Holocarboxylase synthetase: correlation of protein localisation with biological function
Arch. Biochem. Biophys.
496
45-52
2010
Homo sapiens
brenda
Lee, C.K.; Cheong, C.; Jeon, Y.H.
Substrate recognition characteristics of human holocarboxylase synthetase for biotin ligation
Biochem. Biophys. Res. Commun.
391
455-460
2010
Homo sapiens
brenda
Zempleni, J.; Wijeratne, S.S.; Hassan, Y.I.
Biotin
Biofactors
35
36-46
2009
Homo sapiens
brenda
Yokoi, K.; Ito, T.; Maeda, Y.; Nakajima, Y.; Kurono, Y.; Sugiyama, N.; Togari, H.
A case of holocarboxylase synthetase deficiency with insufficient response to prenatal biotin therapy
Brain Dev.
31
775-778
2009
Homo sapiens
brenda
Lee, C.K.; Cheong, C.; Jeon, Y.H.
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein
FEBS Lett.
584
675-680
2010
Homo sapiens
brenda
Tron, C.M.; McNae, I.W.; Nutley, M.; Clarke, D.J.; Cooper, A.; Walkinshaw, M.D.; Baxter, R.L.; Campopiano, D.J.
Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity
J. Mol. Biol.
387
129-146
2009
Aquifex aeolicus (O66837), Aquifex aeolicus
brenda
Wijeratne, S.S.; Camporeale, G.; Zempleni, J.
K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
J. Nutr. Biochem.
21
310-316
2010
Homo sapiens
brenda
Maeda, Y.; Yoshino, T.; Matsunaga, T.
In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide
Appl. Environ. Microbiol.
76
5785-5790
2010
Escherichia coli
brenda
Daniels, K.; Beckett, D.
Biochemical properties and biological function of a monofunctional microbial biotin protein ligase
Biochemistry
49
5358-5365
2010
Pyrococcus horikoshii (O57883)
brenda
Delli-Bovi, T.; Spalding, M.; Prigge, S.
Overexpression of biotin synthase and biotin ligase is required for efficient generation of sulfur-35 labeled biotin in E. coli
BMC Biotechnol.
10
73
2010
Plasmodium falciparum (C6S3D7), Plasmodium falciparum
brenda
Gupta, V.; Gupta, R.; Khare, G.; Salunke, D.; Surolia, A.; Tyagi, A.
Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration
PLoS ONE
5
e9222
2010
Mycobacterium tuberculosis (P96884), Mycobacterium tuberculosis
brenda
Purushothaman, S.; Annamalai, K.; Tyagi, A.; Surolia, A.
Diversity in functional organization of class I and class II biotin protein ligase
PLoS ONE
6
e16850
2011
Escherichia coli, Mycobacterium tuberculosis (P96884)
brenda
Sueda, S.; Tanaka, H.; Yamagishi, M.
A biotin-based protein tagging system
Anal. Biochem.
393
189-195
2009
Sulfurisphaera tokodaii
brenda
Sueda, S.; Shinboku, Y.; Kusaba, T.
An SH2 domain-based tyrosine kinase assay using biotin ligase modified with a terbium(III) complex
Anal. Sci.
29
491-497
2013
Sulfurisphaera tokodaii
brenda
Li, Y.Q.; Sueda, S.; Kondo, H.; Kawarabayasi, Y.
A unique biotin carboxyl carrier protein in archaeon Sulfolobus tokodaii
FEBS Lett.
580
1536-1540
2006
Escherichia coli, Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii 7 (F9VNG7)
brenda
Peters-Wendisch, P.; Stansen, K.C.; Goetker, S.; Wendisch, V.F.
Biotin protein ligase from Corynebacterium glutamicum: role for growth and L: -lysine production
Appl. Microbiol. Biotechnol.
93
2493-2502
2012
Corynebacterium glutamicum (Q8NSG6), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q8NSG6)
brenda
Soares da Costa, T.P.; Tieu, W.; Yap, M.Y.; Pendini, N.R.; Polyak, S.W.; Sejer Pedersen, D.; Morona, R.; Turnidge, J.D.; Wallace, J.C.; Wilce, M.C.; Booker, G.W.; Abell, A.D.
Selective inhibition of biotin protein ligase from Staphylococcus aureus
J. Biol. Chem.
287
17823-17832
2012
Staphylococcus aureus, Staphylococcus aureus ECT-2
brenda
Soares da Costa, T.P.; Yap, M.Y.; Perugini, M.A.; Wallace, J.C.; Abell, A.D.; Wilce, M.C.; Polyak, S.W.; Booker, G.W.
Dual roles of F123 in protein homodimerization and inhibitor binding to biotin protein ligase from Staphylococcus aureus
Mol. Microbiol.
91
110-120
2014
Staphylococcus aureus, Staphylococcus aureus ECT-R2
brenda
Li, Y.; Sousa, R.
Expression and purification of E. coli BirA biotin ligase for in vitro biotinylation
Protein Expr. Purif.
82
162-167
2012
Escherichia coli, Escherichia coli AVB101
brenda
Pendini, N.R.; Yap, M.Y.; Traore, D.A.; Polyak, S.W.; Cowieson, N.P.; Abell, A.; Booker, G.W.; Wallace, J.C.; Wilce, J.A.; Wilce, M.C.
Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target
Protein Sci.
22
762-773
2013
Staphylococcus aureus, Staphylococcus aureus ECT-R2
brenda
Chen, X.; Chou, H.H.; Wurtele, E.S.
Holocarboxylase synthetase 1 physically interacts with histone H3 in Arabidopsis
Scientifica
2013
983501
2013
Arabidopsis thaliana
brenda
Miyao, H.; Ikeda, Y.; Shiraishi, A.; Kawakami, Y.; Sueda, S.
Immobilization of immunoglobulin-G-binding domain of Protein A on a gold surface modified with biotin ligase
Anal. Biochem.
484
113-121
2015
Sulfurisphaera tokodaii (F9VNG7), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VNG7)
brenda
Tieu, W.; Jarrad, A.M.; Paparella, A.S.; Keeling, K.A.; Soares da Costa, T.P.; Wallace, J.C.; Booker, G.W.; Polyak, S.W.; Abell, A.D.
Heterocyclic acyl-phosphate bioisostere-based inhibitors of Staphylococcus aureus biotin protein ligase
Bioorg. Med. Chem. Lett.
24
4689-4693
2014
Staphylococcus aureus
brenda
Lu, W.; Levy, M.; Kincaid, R.; Ellington, A.
Directed evolution of the substrate specificity of biotin ligase
Biotechnol. Bioeng.
111
1071-1081
2014
Escherichia coli
brenda
Wang, Z.; Moslehi-Jenabian, S.; Solem, C.; Jensen, P.
Increased expression of pyruvate carboxylase and biotin protein ligase increases lysine production in a biotin prototrophic Corynebacterium glutamicum strain
Eng. Life Sci.
15
73-82
2015
Bacillus subtilis, Bacillus subtilis 168
-
brenda
Sam, J.; Sharmila, J.
Molecular docking of benzoxazolone and its derivatives against Staphylococcus aureus biotin protein ligase
Int. J. Pharm. Sci. Rev. Res.
32
72-76
2015
Staphylococcus aureus
-
brenda
Bockman, M.R.; Kalinda, A.S.; Petrelli, R.; De la Mora-Rey, T.; Tiwari, D.; Liu, F.; Dawadi, S.; Nandakumar, M.; Rhee, K.Y.; Schnappinger, D.; Finzel, B.C.; Aldrich, C.C.
Targeting Mycobacterium tuberculosis biotin protein ligase (MtBPL) with nucleoside-based bisubstrate adenylation inhibitors
J. Med. Chem.
58
7349-7369
2015
Mycobacterium tuberculosis (I6YFP0), Mycobacterium tuberculosis H37Rv (I6YFP0)
brenda
Feng, Y.; Chin, C.; Chakravartty, V.; Gao, R.; Crispell, E.; Weiss, D.; Cronan, J.
The atypical occurrence of two biotin protein ligases in Francisella novicida is due to distinct roles in virulence and biotin metabolism
mBio
6
e00591
2015
Francisella tularensis subsp. novicida
brenda
Bond, T.E.H.; Sorenson, A.E.; Schaeffer, P.M.
A green fluorescent protein-based assay for high-throughput ligand-binding studies of a mycobacterial biotin protein ligase
Microbiol. Res.
205
35-39
2017
Mycobacterium tuberculosis (P96884), Mycobacterium tuberculosis CDC 1551 (P96884)
brenda
Henke, S.K.; Cronan, J.E.
The Staphylococcus aureus group II biotin protein ligase BirA is an effective regulator of biotin operon transcription and requires the DNA binding domain for full enzymatic activity
Mol. Microbiol.
102
417-429
2016
Staphylococcus aureus (A0A0H3KCT0), Staphylococcus aureus Newman (A0A0H3KCT0)
brenda
Henke, S.; Cronan, J.
Successful conversion of the Bacillus subtilis BirA group II biotin protein ligase into a group I ligase
PLoS ONE
9
e96757
2014
Bacillus subtilis (P0CI75), Bacillus subtilis 168 (P0CI75)
brenda
Ma, Q.; Akhter, Y.; Wilmanns, M.; Ehebauer, M.T.
Active site conformational changes upon reaction intermediate biotinyl-5-AMP binding in biotin protein ligase from Mycobacterium tuberculosis
Protein Sci.
23
932-939
2014
Mycobacterium tuberculosis (I6YFP0), Mycobacterium tuberculosis H37Rv (I6YFP0)
brenda
Paparella, A.; Feng, J.; Blanco-Rodriguez, B.; Feng, Z.; Phetsang, W.; Blaskovich, M.; Cooper, M.; Booker, G.; Polyak, S.; Abell, A.
A template guided approach to generating cell permeable inhibitors of Staphylococcus aureus biotin protein ligase
Tetrahedron
74
1175-1183
2017
Staphylococcus aureus
-
brenda
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