ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis

Biochemistry. 2008 Sep 2;47(35):9054-6. doi: 10.1021/bi8010253. Epub 2008 Aug 8.


Thiamin pyrophosphate is a required cofactor in all organisms. The biosynthesis of thiamin requires the independently synthesized 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate (HMP-PP) and 5-hydroxyethyl-4-methylthiazole phosphate (THZ-P) moieties. In bacteria, the pyrimidine moiety is derived from 5-aminoimidazole ribotide (AIR), and ThiC is the only gene product known to be required for this conversion in vivo. We report here the purification and characterization of the ThiC protein from Salmonella enterica. The data showed this protein generated HMP when AIR, S-adenosylmethionine (AdoMet), and an appropriate reducing agent were present. It is further shown that ThiC carries an oxygen labile [Fe-S] cluster essential for this activity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Diphosphates / metabolism
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / isolation & purification
  • Iron-Sulfur Proteins / metabolism
  • Oxidation-Reduction
  • Pyrimidines / metabolism*
  • Ribonucleotides / metabolism
  • S-Adenosylmethionine / metabolism*
  • Salmonella enterica / metabolism
  • Thiamine / biosynthesis*


  • 4-amino-5-hydroxymethyl-2-methylpyrimidine
  • 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate
  • Bacterial Proteins
  • Diphosphates
  • Iron-Sulfur Proteins
  • Pyrimidines
  • Ribonucleotides
  • ThiC protein, Bacteria
  • aminoimidazole ribotide
  • S-Adenosylmethionine
  • Thiamine