Phosphomethylpyrimidine synthase

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Phosphomethylpyrimidine synthase
4s27.jpg
Phosphomethylpyrimidine synthase dimer, Arabidopsis thaliana
Identifiers
EC number4.1.99.17
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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[edit]

  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 2587053. 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. PMC 2654281. 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. PMC 3147014. PMID 20886485.

External links[edit]