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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
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.
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This record set is specific for:
UNIPROT: O57883
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
biotin ligase, bira protein, biotin-protein ligase, biotin holoenzyme synthetase, bacterial bira biotin ligase, biotin acetyl-coa carboxylase ligase, holocarboxylase synthetase 1, group i biotin protein ligase, biotin:apocarboxylase ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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--protein ligase
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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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HCS
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Synthetase, biotin-[acetyl coenzyme A carboxylase]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37340-95-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-[acetyl CoA carboxylase]
AMP + diphosphate + acetyl CoA carboxylase
show the reaction diagram
no coupling is observed in ATP and biotin binding to the BPL
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O57883_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
235
0
26072
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
51200
sedimentation equilibrium study
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daniels, K.; Beckett, D.
Biochemical properties and biological function of a monofunctional microbial biotin protein ligase
Biochemistry
49
5358-5365
2010
Pyrococcus horikoshii (O57883)
Manually annotated by BRENDA team