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
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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
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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Application
Application on EC 6.3.4.15 - biotin-[biotin carboxyl-carrier protein] ligase
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analysis
diagnostics
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BirA can be useful for specific in vivo labeling of proteins in cell cultures by biotinylation
drug development
synthesis
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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
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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
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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
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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
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development of a high-throughput assay building on the principle of differential scanning fluorimetry of GFP-tagged proteins
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the enzyme is a potential target for anti-mycobacterial drugs
drug development
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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
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the enzyme is a target for the design of effective antifungal drugs
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the enzyme is utilized to synthesize site-specific biotinylated proteins via a biotin acceptor peptide tag
synthesis
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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
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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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