| 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (CofG) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.32 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| 5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase (CofH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.147 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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 | |
| Symbol | CofG |
| InterPro | IPR019939 |
| CofH | |
|---|---|
| Identifiers | |
| Symbol | CofH |
| InterPro | IPR019940 |
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
- ↑ 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.
- ↑ 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.
External links
- 7,8-didemethyl-8-hydroxy-5-deazariboflavin+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)