A unique biotin carboxyl carrier protein in archaeon Sulfolobus tokodaii

FEBS Lett. 2006 Mar 6;580(6):1536-40. doi: 10.1016/j.febslet.2006.01.083. Epub 2006 Feb 3.

Abstract

Biotin carboxyl carrier protein (BCCP) is one subunit or domain of biotin-dependent enzymes. BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL). BCCP carries a characteristic local sequence surrounding the canonical lysine residue, typically -M-K-M-. Archaeon Sulfolobus tokodaii is unique in that its BCCP has serine replaced for the methionine C-terminal to the lysine. This BCCP is biotinylated by its own BPL, but not by Escherichia coli BPL. Likewise, E. coli BCCP is not biotinylated by S. tokodaii BPL, indicating that the substrate specificity is different between the two organisms.

MeSH terms

  • Acetyl-CoA Carboxylase / chemistry*
  • Acetyl-CoA Carboxylase / genetics
  • Acetyl-CoA Carboxylase / isolation & purification
  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / isolation & purification
  • Biotinylation
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / isolation & purification
  • Fatty Acid Synthase, Type II
  • Molecular Sequence Data
  • Substrate Specificity
  • Sulfolobus / enzymology*

Substances

  • Archaeal Proteins
  • Carrier Proteins
  • Fatty Acid Synthase, Type II
  • Acetyl-CoA Carboxylase
  • biotin carboxyl carrier protein