PMID:10470036

Citation	Chapman-Smith, A and Cronan, JE Jr (1999) The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends Biochem. Sci. 24:359-63
Abstract	Biotin is a coenzyme essential to all life forms. The vitamin has biological activity only when covalently attached to certain key metabolic enzymes. Most organisms have only one enzyme for attachment of biotin to other proteins and the sequences of these proteins and their substrate proteins are strongly conserved throughout nature. Structures of both the biotin ligase and the biotin carrier protein domain from Escherichia coli have been determined. These, together with mutational analyses of biotinylated proteins, are beginning to elucidate the exceptional specificity of this protein modification.
Links	PubMed
Keywords	Acetyl-CoA Carboxylase/chemistry; Acetyl-CoA Carboxylase/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biotin/metabolism; Carbon-Nitrogen Ligases/chemistry; Carbon-Nitrogen Ligases/metabolism; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Fatty Acid Synthetase Complex, Type II; Models, Molecular; Protein Conformation; Protein Processing, Post-Translational; Repressor Proteins; Transcription Factors
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