6.3.4.15: biotin-[biotin carboxyl-carrier protein] ligase
This is an abbreviated version!
For detailed information about biotin-[biotin carboxyl-carrier protein] ligase, go to the full flat file.
Word Map on EC 6.3.4.15
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6.3.4.15
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biotinylation
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streptavidin
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bioid
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proximity-dependent
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bap
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avidin
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avitag
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streptavidin-coated
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biotin-dependent
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transcarboxylase
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proximity-labeling
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biotinyl-5\'-amp
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drug development
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unbiotinylated
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15-amino
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biotin-streptavidin
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diagnostics
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analysis
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synthesis
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carboxylases
- 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
-
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
Synonyms
Acetyl CoA holocarboxylase synthetase, Acetyl coenzyme A holocarboxylase synthetase, bacterial BirA biotin ligase, biotin acetyl-CoA carboxylase ligase, Biotin holoenzyme synthetase, biotin ligase, biotin protein ligase, Biotin--protein ligase, biotin-protein ligase, Biotin-[acetyl coenzyme A carboxylase] synthetase, Biotin-[acetyl-CoA carboxylase] synthetase, Biotin:apocarboxylase ligase, BirA, BirA protein, BPL, group I biotin protein ligase, HCS, Holocarboxylase synthetase, holocarboxylase synthetase 1, More, STK_15250, Synthetase, biotin-[acetyl coenzyme A carboxylase], yBL
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Subunits
Subunits on EC 6.3.4.15 - biotin-[biotin carboxyl-carrier protein] ligase
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dimer
homodimer
monomer
additional information
dimer
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2 * 26071 recombinant enzyme, SDS-PAGE and amino acid sequence calculation
dimer
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the functional unit is a dimer, a subunit contains a catalytic N-terminal domain and a C-terminal domain, structure analysis
dimer
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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
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2 * 26071 recombinant enzyme, SDS-PAGE and amino acid sequence calculation
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dimer
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the functional unit is a dimer, a subunit contains a catalytic N-terminal domain and a C-terminal domain, structure analysis
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dimer
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the protein is a constitutive dimer, i.e. dimerises independently of biotin binding
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ligand-free structure, and biotin-ATP intermediate complex of the enzyme, comparison of wild-type and mutant structures, overview
additional information
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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
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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
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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
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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
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acetyl-CoA carboxylase biotinyl domain structure analysis, overview
additional information
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acetyl-CoA carboxylase biotinyl domain structure analysis, overview
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additional information
biotin-protein-ligase/holo-biotin-carboxyl-carrier-protein complex
additional information
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biotin-protein-ligase/holo-biotin-carboxyl-carrier-protein complex
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