- Coenzyme F420 hydrogenase
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coenzyme F420 hydrogenase Identifiers EC number 1.12.98.1 CAS number 9027-05-8 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 / EGO Search PMC articles PubMed articles In enzymology, a coenzyme F420 hydrogenase (EC 1.12.98.1) is an enzyme that catalyzes the chemical reaction
- H2 + coenzyme F420 reduced coenzyme F420
Thus, the two substrates of this enzyme are H2 and coenzyme F420, whereas its product is reduced coenzyme F420.
This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with other, known, acceptors. The systematic name of this enzyme class is hydrogen:coenzyme F420 oxidoreductase. Other names in common use include 8-hydroxy-5-deazaflavin-reducing hydrogenase, F420-reducing hydrogenase, and coenzyme F420-dependent hydrogenase. This enzyme participates in folate biosynthesis. It has 3 cofactors: iron, nickel, and deazaflavin.
References
- Adams MWW, Mortenson LE and Chen J-S (1981). "Hydrogenase". Biochim. Biophys. Acta 594: 105–176.
- Yamazaki S (1982). "A selenium-containing hydrogenase from Methanococcus vannielii Identification of the selenium moiety as a selenocysteine residue". J. Biol. Chem. 257 (14): 7926–9. PMID 6211447.
- Fox JA, Livingston DJ, Orme-Johnson WH, Walsh CT (1987). "8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization". Biochemistry. 26 (14): 4219–27. doi:10.1021/bi00388a007. PMID 3663585.
- Muth E, Morschel E, Klein A (1987). "Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae". Eur. J. Biochem. 169 (3): 571–7. doi:10.1111/j.1432-1033.1987.tb13647.x. PMID 3121317.
- Baron SF, Ferry JG (1989). "Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum". J. Bacteriol. 171 (7): 3846–53. PMC 210134. PMID 2738024. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=210134.
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