The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity

Anne Chapman-Smith, John E Cronan

Research output: Contribution to journalReview article

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. Copyright (C) 1999 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)359-363
Number of pages5
JournalTrends in Biochemical Sciences
Volume24
Issue number9
DOIs
StatePublished - Sep 1 1999

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Biotinylation
Staphylococcal Protein A
Post Translational Protein Processing
Biotin
Proteins
Coenzymes
Enzymes
Ligases
Bioactivity
Vitamins
Escherichia coli
Carrier Proteins
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

The enzymatic biotinylation of proteins : A post-translational modification of exceptional specificity. / Chapman-Smith, Anne; Cronan, John E.

In: Trends in Biochemical Sciences, Vol. 24, No. 9, 01.09.1999, p. 359-363.

Research output: Contribution to journalReview article

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