Phosphomethylpyrimidine synthase

Phosphomethylpyrimidine synthase
Identifiers
EC number 4.1.99.17
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Phosphomethylpyrimidine synthase (EC 4.1.99.17, thiC (gene)) is an enzyme with systematic name 5-amino-1-(5-phospho-D-ribosyl)imidazole formate-lyase (decarboxylating, 4-amino-2-methyl-5-phosphomethylpyrimidine-forming).[1][2][3] This enzyme catalyses the following chemical reaction

5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO

This enzyme binds a 4Fe-4S cluster.

References

  1. Chatterjee, A.; Li, Y.; Zhang, Y.; Grove, T.L.; Lee, M.; Krebs, C.; Booker, S.J.; Begley, T.P.; Ealick, S.E. (2008). "Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily". Nat. Chem. Biol. 4: 758–765. doi:10.1038/nchembio.121. PMC 2587053Freely accessible. PMID 18953358.
  2. Martinez-Gomez, N.C.; Poyner, R.R.; Mansoorabadi, S.O.; Reed, G.H.; Downs, D.M. (2009). "Reaction of AdoMet with ThiC generates a backbone free radical". Biochemistry. 48 (2): 217–219. doi:10.1021/bi802154j. PMID 19113839.
  3. Chatterjee, A.; Hazra, A.B.; Abdelwahed, S.; Hilmey, D.G.; Begley, T.P. (2010). "A "radical dance" in thiamin biosynthesis: mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase". Angew. Chem. Int. Ed. Engl. 49 (46): 8653–8656. doi:10.1002/anie.201003419. PMID 20886485.
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