Biology: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 [math]\displaystyle{ \rightleftharpoons }[/math] 4-amino-2-methyl-5-phosphomethylpyrimidine + 5′-deoxyadenosine + L-methionine + formate + CO

This enzyme binds a 4Fe-4S cluster.

Pyrimidine biosynthesis.svg

The starting material is 5-aminoimidazole ribotide, which undergoes a rearrangement reaction via radical intermediates which incorporate the blue, green and red fragments shown into the product.[3][4]

References

  1. "Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily". Nature Chemical Biology 4 (12): 758–65. December 2008. doi:10.1038/nchembio.121. PMID 18953358. 
  2. "Reaction of AdoMet with ThiC generates a backbone free radical". Biochemistry 48 (2): 217–9. January 2009. doi:10.1021/bi802154j. PMID 19113839. 
  3. 3.0 3.1 "A "radical dance" in thiamin biosynthesis: mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase". Angewandte Chemie 49 (46): 8653–6. November 2010. doi:10.1002/anie.201003419. PMID 20886485. 
  4. Begley, Tadhg P. (2006). "Cofactor biosynthesis: An organic chemist's treasure trove". Natural Product Reports 23 (1): 15–18. doi:10.1039/b207131m. PMID 16453030. 

External links

External links