In vivo enzymatic protein biotinylation

Biomol Eng. 1999 Dec 31;16(1-4):119-25. doi: 10.1016/s1050-3862(99)00046-7.

Abstract

Biotin is biologically active only when protein-bound and is covalently attached to a class of important metabolic enzymes, the biotin carboxylases and decarboxylases. Biotinylation is a relatively rare modification, with between one and five biotinylated protein species found in different organisms. We discuss the mechanism and structures involved in this extraordinarily specific protein modification and its exploitation in tagging recombinant proteins.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Biotin / metabolism*
  • Biotinylation / methods
  • Carbon-Nitrogen Ligases / genetics
  • Carbon-Nitrogen Ligases / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Engineering
  • Protein Structure, Tertiary
  • Proteins / metabolism*
  • Recombinant Proteins / metabolism
  • Repressor Proteins*
  • Sequence Homology, Amino Acid
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Proteins
  • Recombinant Proteins
  • Repressor Proteins
  • Transcription Factors
  • Biotin
  • Carbon-Nitrogen Ligases
  • birA protein, E coli