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Information on EC 6.3.4.15 - biotin-[biotin carboxyl-carrier protein] ligase
for references in articles please use BRENDA:EC6.3.4.15
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.4 Other carbon-nitrogen ligases
6.3.4.15 biotin-[biotin carboxyl-carrier protein] ligase
IUBMB 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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 6.3.4.15
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biotinylation
- streptavidin
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bioid
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proximity-dependent
- bap
- avidin
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avitag
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streptavidin-coated
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biotin-dependent
- transcarboxylase
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proximity-labeling
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biotinyl-5\'-amp
- drug development
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unbiotinylated
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15-amino
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biotin-streptavidin
- diagnostics
- analysis
- synthesis
- carboxylases
Reaction Schemes
showSynonyms
biotin ligase, bira protein, biotin-protein ligase, biotin holoenzyme synthetase, bacterial bira biotin ligase, biotin acetyl-coa carboxylase ligase, biotin:apocarboxylase ligase, holocarboxylase synthetase 1, group i biotin protein ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acetyl CoA holocarboxylase synthetase
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Acetyl coenzyme A holocarboxylase synthetase
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Biotin holoenzyme synthetase
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biotin ligase
biotin protein ligase
Biotin--protein ligase
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biotin-protein ligase
Biotin-[acetyl coenzyme A carboxylase] synthetase
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Biotin-[acetyl-CoA carboxylase] synthetase
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Biotin:apocarboxylase ligase
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BirA
BPL
HCS
Holocarboxylase synthetase
STK_15250
Synthetase, biotin-[acetyl coenzyme A carboxylase]
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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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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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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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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
biotin-carboxyl carrier protein assembly
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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
LITERATURE
COMMENTARY
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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Substrates: i.e. reaction of acetylene derivative of biotin and an azide-functionalized adenine
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(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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Substrates: i.e. reaction of acetylene derivative of biotin and an azide-functionalied analogue of the fluorophore nitrobenzofurazan
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ATP + biotin + apo-[acetyl CoA carboxylase]
AMP + diphosphate + acetyl CoA carboxylase
Substrates: no coupling is observed in ATP and biotin binding to the BPL
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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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Substrates: cytoplasmic acetyl-CoA carboxylase isozyme
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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
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Substrates: 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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Substrates: -
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ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
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Substrates: -
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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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Substrates: 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
Substrates: 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
?
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Substrates: the biotinylated product, holo biotin carboxyl carrier protein, forms a stable complex with the enzyme, which barely dissociates at room temperature
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ATP + biotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + biotinylated CGGGSGGGSGLNDIFEAQKIEWH
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Substrates: -
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ATP + biotin + chimeric protein of glutathione S-transferase and green fluorescence protein with biotin carboxyl carrier proteinDelta100
?
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Substrates: -
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ATP + biotin + fluorescein-labeled peptide 85-11
ADP + diphosphate + biotinyl-fluorescein-labeled peptide 85-11
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Substrates: 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
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ATP + biotin + GLNDIFEAQKIEWH
AMP + diphosphate + biotinylated GLNDIFEAQKIEWH
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Substrates: i.e. Schatz' peptide, synthetic biotinable minimal peptide
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ATP + biotin + yeast acceptor peptide
?
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Substrates: -
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ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine
AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
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Substrates: ATP in form of MgATP2-
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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
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Substrates: 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 + [Escherichia coli apo-biotin-carboxyl-carrier-protein]-L-lysine
AMP + diphosphate + [Escherichia coli biotin-carboxyl-carrier-protein]-biotinyl-L-lysine
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Substrates: 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)]
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Substrates: -
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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)]
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Substrates: -
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ATP + desthiobiotin + CGGGSGGGSGLNDIFEAQKIEWH
AMP + diphosphate + desthiobiotinylated CGGGSGGGSGLNDIFEAQKIEWH
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Substrates: -
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ATP + desthiobiotin azide + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + desthiobiotin azide-containing [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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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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Substrates: recombinant Saccharomyces cerevisiae cells
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avitagged BirA + biotin + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
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Substrates: the recombinant avitagged enzyme biotinylates itself at the avitag sequence
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biotin + ATP
biotinyl-5'-AMP + diphosphate
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Substrates: first half-reaction of BPL
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biotin + ATP + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: 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
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D-biotin + ATP
biotinyl-5'-AMP + diphosphate
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Substrates: first half-reaction of BPL
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ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
Substrates: AccB, i.e. acetyl-CoA carboxylase biotin carboxyl carrier protein biotin attachment domain
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ATP + biotin + AccB-86
AMP + diphosphate + biotinylated AccB-86
Substrates: AccB, i.e. acetyl-CoA carboxylase biotin carboxyl carrier protein biotin attachment domain
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ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
Substrates: -
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ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
Substrates: -
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ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
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Substrates: mitochondrial acetyl-CoA carboxylase isozyme
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ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
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Substrates: 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
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ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
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Substrates: 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
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ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
Substrates: -
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ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
Substrates: 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
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ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: determination of the biotin domains of acetyl-CoA carboxylase, ACC
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: determination of the biotin domains of the pyruvate carboxylase, PC, of the organism, substrate is peptide fragment CaPC115 as GST-tagged recombinant protein, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: BPL is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: determination of the biotin domains of acetyl-CoA carboxylase, ACC
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: determination of the biotin domains of the pyruvate carboxylase, PC, of the organism, substrate is peptide fragment CaPC115 as GST-tagged recombinant protein, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: biotin protein ligase, BPL required to complete acetyl-CoA carboxĀylase's capability for fatty acid biosynthesis
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Substrates: 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
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Substrates: conformational changes occur upon biotin binding. Structure-function relationship, modelling, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: incorporation of biotin into apo-carboxyl carrier protein, a subunit of acetyl-CoA carboxylase from E. coli
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: 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
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: 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
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: biotinylation site determination, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: biotinylation site determination, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: overall reaction
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: 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
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: structure-function relationship, modelling, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: structure-function relationship, modelling, overview
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: all biotin-dependent enzymes utilise the enzyme-bound biotin group for the transfer of CO2 between metabolites
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: -
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ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
Substrates: -
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ATP + biotin + apo-[biotin carboxyl carrier protein]
AMP + diphosphate + biotinylated biotin carboxyl carrier protein
Substrates: -
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ATP + biotin + Avi-tagged thioredoxin
?
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Substrates: biotin ligase site-specifically biotinylates a lysine side chain within a 15-amino acid acceptor peptide (also known as Avi-tag)
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ATP + biotin + Avi-tagged thioredoxin
?
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Substrates: biotin ligase site-specifically biotinylates a lysine side chain within a 15-amino acid acceptor peptide (also known as Avi-tag)
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ATP + biotin + BLAP
AMP + diphosphate + biotinylated BLAP
Substrates: BLAP, i.e. biotin/lipoyl attachment protein
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ATP + biotin + BLAP
AMP + diphosphate + biotinylated BLAP
Substrates: BLAP, i.e. biotin/lipoyl attachment protein
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + protein p67
AMP + diphosphate + biotinyl-protein p67
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Substrates: -
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ATP + biotin + PyC-77
AMP + diphosphate + biotinylated PyC-77
Substrates: Pyc-77, i.e. pyruvate carboxylase biotin attachment domain
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ATP + biotin + PyC-77
AMP + diphosphate + biotinylated PyC-77
Substrates: Pyc-77, i.e. pyruvate carboxylase biotin attachment domain
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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
Substrates: 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
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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
Substrates: the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
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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
Substrates: the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
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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
Substrates: 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
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ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
Substrates: 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
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ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
Substrates: the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
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ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
Substrates: the enzyme from Sulfolobus tokodaii cannot use wild-type biotin carboxyl carrier protein from Escherichia coli as a substrate
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ATP + biotin + [Sulfolobus tokodaii apo-biotin-carboxyl-carrier-protein]-lysine
AMP + diphosphate + [Sulfolobus tokodaii biotin-carboxyl-carrier-protein]-biotinyllysine
Substrates: 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
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avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
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Substrates: recombinant Saccharomyces cerevisiae cells
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avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
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Substrates: recombinant avitag-tagged maltose-binding protein
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biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
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Substrates: 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
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biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
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Substrates: 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
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additional information
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Substrates: evidence for a direct role of the biotin-[acetyl-CoA-carboxylase] ligase in repression of the biotin operon in Escherichia coli
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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-
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Substrates: the enzyme site-specifically biotinylates proteins via a biotin acceptor peptide tag
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additional information
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Substrates: does not use yeast acceptor peptide as a substrate
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additional information
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Substrates: 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
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additional information
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Substrates: Escherichia coli enzyme undergoes self-biotinylation
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additional information
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Substrates: no activity with protein p67
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additional information
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-
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
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additional information
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Substrates: the 4'-hydroxyazobenzene-2-carboxylic acid dye assay can be used to quantify biotin
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additional information
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Substrates: the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: enzyme is not able to biotinylate Schatz' minimal peptide GLNDIFEAQKIEWH
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additional information
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Substrates: structural features influencing the reaction mechanism, overview
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additional information
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Substrates: structural features influencing the reaction mechanism, overview
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additional information
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Substrates: biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase
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additional information
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Substrates: biotin protein ligase is a bifunctional protein, possessing both biotin ligase and transcription repressor activities
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additional information
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Substrates: biotin protein ligase is a bifunctional protein, possessing both biotin ligase and transcription repressor activities
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additional information
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Substrates: 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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
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Substrates: cytoplasmic acetyl-CoA carboxylase isozyme
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ATP + biotin + apo-[acetyl-CoA carboxylase 2]
AMP + diphosphate + acetyl-CoA carboxylase 2
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Substrates: mitochondrial acetyl-CoA carboxylase isozyme
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
-
Substrates: -
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avitag-tagged maltose-binding protein + biotin + ATP
maltose-binding protein-avitag-biotin + AMP + diphosphate
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Substrates: recombinant Saccharomyces cerevisiae cells
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avitagged BirA + biotin + ATP
BirA-avitag-biotin + AMP + diphosphate
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Substrates: recombinant Saccharomyces cerevisiae cells
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biotin + ATP
biotinyl-5'-AMP + diphosphate
-
Substrates: first half-reaction of BPL
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biotinyl-5'-AMP + apocarboxylase
holocarboxylase + AMP
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Substrates: 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
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ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
Substrates: -
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ATP + biotin + apo-[acetyl-CoA carboxylase]
AMP + diphosphate + acetyl-CoA carboxylase
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Substrates: -
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ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
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Substrates: BPL is an essential enzyme responsible