biotin---[acetyl-CoA-carboxylase] ligase
biotin-[acetyl-CoA carboxylase] synthetase
biotin-[acetyl coenzyme A carboxylase] synthetase
acetyl coenzyme A holocarboxylase synthetase
Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
[Acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
Energetic methods to study bifunctional biotin operon repressor.
Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase.
The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity.
Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
The biotin repressor: modulation of allostery by corepressor analogs.
This protein is bifunctional, acting both as a biotin-transferring enzyme and as a transcriptional regulator (see [1]). As the biotin-transferring enzyme, this protein catalyzes two successive reactions. The first reaction is transfer of adenylate from ATP to the carboxylate of biotin, which results in the formation of biotinyl-5'-AMP, releasing pyrophosphate. The second reaction is transfer of the biotin moiety from the intermediate, biotinyl-5'-AMP, to the correct lysine residue of protein substrate, acetyl-CoA carboxylase. However, the detailed mechanism of catalysis has not been elucidated.