7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (CofG)
Identifiers
EC no.4.3.1.32
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins
5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase (CofH)
Identifiers
EC no.2.5.1.147
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (EC 4.3.1.32, FO synthase) and 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase (EC 2.5.1.147) are two enzymes always complexed together to achieve synthesis of FO, a precursor to Coenzyme F420. Their systematic names are 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil ammonia-lyase (7,8-didemethyl-8-hydroxy-5-deazariboflavin-forming) and 5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase respectively.[1][2] The enzymes catalyse the following chemical reactions:

(2.5.1.147) 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosin
(4.3.1.32) 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine

Enzyme 2.5.1.147 binds a 4Fe-4S cluster. The condensation reaction is initiated by the 5'-deoxyadenosyl radical. The complex was formerly named as a single entity under EC 2.5.1.77.

CofG
Identifiers
SymbolCofG
InterProIPR019939
CofH
Identifiers
SymbolCofH
InterProIPR019940

All members of these enzymes belong to a single clade of the CofH (2.5.1.147) and CofG (4.3.1.32) families, sharing a TIM barrel structure. The two EC numbers represent discrete steps in this reaction. Some enzyme complexes have CofG and CofH (subunits 1 and 2) in different chains assembled into a heterodimer, while others like the bifunctional fbiC has the two domains on one single chain.

References

  1. Graham DE, Xu H, White RH (December 2003). "Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F(420) biosynthesis". Archives of Microbiology. 180 (6): 455–64. doi:10.1007/s00203-003-0614-8. PMID 14593448.
  2. Choi KP, Kendrick N, Daniels L (May 2002). "Demonstration that fbiC is required by Mycobacterium bovis BCG for coenzyme F(420) and FO biosynthesis". Journal of Bacteriology. 184 (9): 2420–8. doi:10.1128/JB.184.9.2420-2428.2002. PMC 134996. PMID 11948155.
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