Biotin protein ligase from Saccharomyces cerevisiae. The N-terminal domain is required for complete activity.
about
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate proteinBiotin Protein Ligase Is a Target for New AntibacterialsProtein biotinylation visualized by a complex structure of biotin protein ligase with a substrateSelective inhibition of Biotin Protein Ligase from Staphylococcus aureusThe C-terminal domain of biotin protein ligase from E. coli is required for catalytic activityMutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains.Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins.Simplified approaches for the development of an ELISA to detect circulating autoantibodies to p53 in cancer patientsLigand specificity of group I biotin protein ligase of Mycobacterium tuberculosisBiotin analogues with antibacterial activity are potent inhibitors of biotin protein ligase.The switch regulating transcription of the Escherichia coli biotin operon does not require extensive protein-protein interactions.Biotinylation, a post-translational modification controlled by the rate of protein-protein association.Improved Synthesis of Biotinol-5'-AMP: Implications for Antibacterial Discovery.Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation.Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species.Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein.Biotinylation in the hyperthermophile Aquifex aeolicus.A novel molecular mechanism to explain biotin-unresponsive holocarboxylase synthetase deficiency.Dual roles of F123 in protein homodimerization and inhibitor binding to biotin protein ligase from Staphylococcus aureus.Biotin sensing in Saccharomyces cerevisiae is mediated by a conserved DNA element and requires the activity of biotin-protein ligase.New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket of Staphylococcus aureus Biotin Protein Ligase.
P2860
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P2860
Biotin protein ligase from Saccharomyces cerevisiae. The N-terminal domain is required for complete activity.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Biotin protein ligase from Sac ...... equired for complete activity.
@ast
Biotin protein ligase from Sac ...... equired for complete activity.
@en
Biotin protein ligase from Sac ...... equired for complete activity.
@nl
type
label
Biotin protein ligase from Sac ...... equired for complete activity.
@ast
Biotin protein ligase from Sac ...... equired for complete activity.
@en
Biotin protein ligase from Sac ...... equired for complete activity.
@nl
prefLabel
Biotin protein ligase from Sac ...... equired for complete activity.
@ast
Biotin protein ligase from Sac ...... equired for complete activity.
@en
Biotin protein ligase from Sac ...... equired for complete activity.
@nl
P2093
P2860
P3181
P356
P1476
Biotin protein ligase from Sac ...... equired for complete activity.
@en
P2093
A Chapman-Smith
J C Wallace
P J Brautigan
S W Polyak
P2860
P304
P3181
P356
10.1074/JBC.274.46.32847
P407
P577
1999-11-12T00:00:00Z