| EC |
4.3.1.32 |
| Accepted name: |
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase |
| Reaction: |
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 |
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For diagram of coenzyme F420 biosynthesis, click here |
| Other name(s): |
FO synthase; fbiC (gene name) (ambiguous); cofG (gene name) |
| Systematic name: |
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil ammonia-lyase (7,8-didemethyl-8-hydroxy-5-deazariboflavin-forming) |
| Comments: |
The enzyme produces the 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) precursor of factor 420 (coenzyme F420), a metabolite found in methanogens and in various actinobacteria. FO is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase, is a radical SAM enzyme that uses the 5′-deoxyadenosyl radical to catalyse the condensation reaction. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Decamps, L., Philmus, B., Benjdia, A., White, R., Begley, T.P. and Berteau, O. Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. J. Am. Chem. Soc. 134 (2012) 18173–18176. [DOI] [PMID: 23072415] |
| 2. |
Philmus, B., Decamps, L., Berteau, O. and Begley, T.P. Biosynthetic versatility and coordinated action of 5′-deoxyadenosyl radicals in deazaflavin biosynthesis. J. Am. Chem. Soc. 137 (2015) 5406–5413. [DOI] [PMID: 25781338] |
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| [EC 4.3.1.32 created 2010 as EC 2.5.1.77, part transferred 2018 to EC 4.3.1.32] |
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