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Class of enzymes From Wikipedia, the free encyclopedia
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:
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase (CofG) | |||||||||
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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 | ||||||||
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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 | ||||||||
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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.
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.
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