Molecular biology of biotin attachment to proteins

J Nutr. 1999 Feb;129(2S Suppl):477S-484S. doi: 10.1093/jn/129.2.477S.

Abstract

Enzymatic attachment of biotin to proteins requires the interaction of a distinct domain of the acceptor protein (the "biotin domain") with the enzyme, biotin protein ligase, that catalyzes this essential and rare post-translational modification. Both biotin domains and biotin protein ligases are very strongly conserved throughout biology. This review concerns the protein structures and mechanisms involved in the covalent attachment of biotin to proteins.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacteria / enzymology
  • Bacteria / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Biotin / biosynthesis
  • Biotin / metabolism*
  • Biotinylation
  • Carbon-Nitrogen Ligases / chemistry
  • Carbon-Nitrogen Ligases / metabolism
  • Escherichia coli Proteins*
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Proteins / metabolism*
  • Repressor Proteins*
  • Sequence Alignment
  • Transcription Factors*

Substances

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