EC Number   |
Application |
Reference |
|---|
    6.3.4.15 | 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 |
1445 |
| 6.3.4.15 | 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 |
1446 |
| 6.3.4.15 | analysis |
development of a high-throughput assay building on the principle of differential scanning fluorimetry of GFP-tagged proteins |
-, 745716 |
| 6.3.4.15 | 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 |
746524 |
| 6.3.4.15 | 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 |
723946 |
| 6.3.4.15 | diagnostics |
BirA can be useful for specific in vivo labeling of proteins in cell cultures by biotinylation |
694319 |
| 6.3.4.15 | drug development |
the enzyme is a potential target for anti-mycobacterial drugs |
689712 |
| 6.3.4.15 | drug development |
the enzyme is a target for the design of effective antifungal drugs |
-, 690627 |
| 6.3.4.15 | drug development |
the enzyme is a target for the design of effective antitubercular drugs |
690261 |
| 6.3.4.15 | 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 |
713831 |
