The Enzyme Database

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EC 1.1.98.2     
Accepted name: glucose-6-phosphate dehydrogenase (coenzyme-F420)
Reaction: D-glucose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
Other name(s): coenzyme F420-dependent glucose-6-phosphate dehydrogenase; F420-dependent glucose-6-phosphate dehydrogenase; FGD1; Rv0407; F420-dependent glucose-6-phosphate dehydrogenase 1
Systematic name: D-glucose-6-phosphate:F420 1-oxidoreductase
Comments: The enzyme is very specific for D-glucose 6-phosphate. No activity with NAD+, NADP+, FAD and FMN [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Purwantini, E. and Daniels, L. Purification of a novel coenzyme F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis. J. Bacteriol. 178 (1996) 2861–2866. [DOI] [PMID: 8631674]
2.  Bashiri, G., Squire, C.J., Baker, E.N. and Moreland, N.J. Expression, purification and crystallization of native and selenomethionine labeled Mycobacterium tuberculosis FGD1 (Rv0407) using a Mycobacterium smegmatis expression system. Protein Expr. Purif. 54 (2007) 38–44. [DOI] [PMID: 17376702]
3.  Purwantini, E., Gillis, T.P. and Daniels, L. Presence of F420-dependent glucose-6-phosphate dehydrogenase in Mycobacterium and Nocardia species, but absence from Streptomyces and Corynebacterium species and methanogenic Archaea. FEMS Microbiol. Lett. 146 (1997) 129–134. [DOI] [PMID: 8997717]
[EC 1.1.98.2 created 2010 as EC 1.1.99.34, transferred 2011 to EC 1.1.98.2]
 
 
EC 1.1.98.4     
Accepted name: F420H2:quinone oxidoreductase
Reaction: a quinol + oxidized coenzyme F420 = a quinone + reduced coenzyme F420
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): FqoF protein
Systematic name: quinol:coenzyme-F420 oxidoreductase
Comments: An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and Archaeoglobus fulgidus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bruggemann, H., Falinski, F. and Deppenmeier, U. Structure of the F420H2:quinone oxidoreductase of Archaeoglobus fulgidus identification and overproduction of the F420H2-oxidizing subunit. Eur. J. Biochem. 267 (2000) 5810–5814. [DOI] [PMID: 10971593]
2.  Kunow, J., Linder, D., Stetter, K.O. and Thauer, R.K. F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters. Eur. J. Biochem. 223 (1994) 503–511. [DOI] [PMID: 8055920]
3.  Abken, H.-J. and Deppenmeier, U. Purification and properties of an F420H2 dehydrogenase from Methanosarcina mazei Gö1. FEMS Microbiol. Lett. 154 (1997) 231–237.
[EC 1.1.98.4 created 2013]
 
 
EC 1.1.98.5     
Accepted name: secondary-alcohol dehydrogenase (coenzyme-F420)
Reaction: R-CHOH-R′ + oxidized coenzyme F420 = R-CO-R′ + reduced coenzyme F420
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): F420-dependent alcohol dehydrogenase; secondary alcohol:F420 oxidoreductase; F420-dependent secondary alcohol dehydrogenase
Systematic name: secondary-alcohol:coenzyme F420 oxidoreductase
Comments: The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bleicher, K. and Winter, J. Purification and properties of F420- and NADP+-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols. Eur. J. Biochem. 200 (1991) 43–51. [DOI] [PMID: 1879431]
2.  Aufhammer, S.W., Warkentin, E., Berk, H., Shima, S., Thauer, R.K. and Ermler, U. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure 12 (2004) 361–370. [DOI] [PMID: 15016352]
[EC 1.1.98.5 created 2013]
 
 
EC 1.1.99.34      
Transferred entry: glucose-6-phosphate dehydrogenase (coenzyme-F420). As the acceptor is now known, the enzyme has been transferred to EC 1.1.98.2, glucose-6-phosphate dehydrogenase (coenzyme-F420)
[EC 1.1.99.34 created 2010, deleted 2011]
 
 
EC 1.2.99.9      
Transferred entry: formate dehydrogenase (coenzyme F420). Now EC 1.17.98.3, formate dehydrogenase (coenzyme F420)
[EC 1.2.99.9 created 2014, deleted 2017]
 
 
EC 1.3.8.17     
Accepted name: dehydro coenzyme F420 reductase
Reaction: oxidized coenzyme F420-0 + FMN = dehydro coenzyme F420-0 + FMNH2
Glossary: dehydro coenzyme F420-0 = 2-{[5-deoxy-5-(8-hydroxy-2,4-dioxopyrimidino[4,5-b]quinolin-10(2H)-yl)-L-ribityloxy]hydroxyphosphoryloxy}prop-2-enoate
Other name(s): fbiB (gene name)
Systematic name: oxidized coenzyme F420-0:FMN oxidoreductase
Comments: This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria. In some eubacteria the enzyme is multifunctional, also catalysing the activities of EC 6.3.2.31, coenzyme F420-0:L-glutamate ligase, and EC 6.3.2.34, coenzyme F420-1:γ-L-glutamate ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bashiri, G., Antoney, J., Jirgis, E.NM., Shah, M.V., Ney, B., Copp, J., Stuteley, S.M., Sreebhavan, S., Palmer, B., Middleditch, M., Tokuriki, N., Greening, C., Scott, C., Baker, E.N. and Jackson, C.J. A revised biosynthetic pathway for the cofactor F420 in prokaryotes. Nat. Commun. 10:1558 (2019). [DOI] [PMID: 30952857]
[EC 1.3.8.17 created 2021]
 
 
EC 1.3.98.4     
Accepted name: 5a,11a-dehydrotetracycline reductase
Reaction: tetracycline + oxidized coenzyme F420 = 5a,11a-dehydrotetracycline + reduced coenzyme F420
For diagram of tetracycline biosynthesis, click here
Other name(s): oxyR (gene name); 12-dehydrotetracycline dehydrogenase; dehydrooxytetracycline dehydrogenase; 12-dehydrotetracycline reductase
Systematic name: tetracycline:coenzyme F420 dehydrogenase
Comments: The enzyme, characterized from the bacteria Streptomyces aureofaciens and Streptomyces rimosus, catalyses the last step in the biosynthesis of the tetracycline antibiotics tetracycline and oxytetracycline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  McCormick, J.R.D., Hirsch, U., Sjolander, N.O. and Doerschuk, A.P. Cosynthesis of tetracyclines by pairs of Streptomyces aureofaciens mutants. J. Am. Chem. Soc. 82 (1960) 5006–5007.
2.  Miller, P.A., Sjolander, N.O., Nalesnyk, S., Arnold, N., Johnson, S., Doerschuk, A.P. and McCormick, J.R.D. Cosynthetic factor I, a factor involved in hydrogen-transfer in Streptomyces aureofaciens. J. Am. Chem. Soc. 82 (1960) 5002–5003.
3.  McCormick, J.R.D. and Morton, G.O. Identity of cosynthetic factor I of Streptomyces aureofaciens and fragment FO from coenzyme F420 of Methanobacterium species. J. Am. Chem. Soc. 104 (1982) 4014–4015.
4.  Wang, P., Bashiri, G., Gao, X., Sawaya, M.R. and Tang, Y. Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis. J. Am. Chem. Soc. 135 (2013) 7138–7141. [DOI] [PMID: 23621493]
[EC 1.3.98.4 created 2016]
 
 
EC 1.5.1.40     
Accepted name: 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
Reaction: reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+
For diagram of coenzyme F420 biosynthesis, click here
Other name(s): 8-OH-5dFl:NADPH oxidoreductase
Systematic name: reduced coenzyme F420:NADP+ oxidoreductase
Comments: The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Eker, A.P., Hessels, J.K. and Meerwaldt, R. Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus. Biochim. Biophys. Acta 990 (1989) 80–86. [DOI] [PMID: 2492438]
[EC 1.5.1.40 created 2011]
 
 
EC 1.5.3.22     
Accepted name: coenzyme F420H2 oxidase
Reaction: 2 reduced coenzyme F420 + O2 = 2 oxidized coenzyme F420 + 2 H2O
For diagram of coenzyme F420 biosynthesis, click here
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): FprA
Systematic name: reduced coenzyme F420:oxygen oxidoreductase
Comments: The enzyme contains FMN and a binuclear iron center. The enzyme from the archaeon Methanothermobacter marburgensis is Si-face specific with respect to C-5 of coenzyme F420 [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Seedorf, H., Dreisbach, A., Hedderich, R., Shima, S. and Thauer, R.K. F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification. Arch. Microbiol. 182 (2004) 126–137. [DOI] [PMID: 15340796]
2.  Seedorf, H., Kahnt, J., Pierik, A.J. and Thauer, R.K. Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from methanogenic Archaea as determined by mass spectrometry. FEBS J. 272 (2005) 5337–5342. [DOI] [PMID: 16218963]
3.  Seedorf, H., Hagemeier, C.H., Shima, S., Thauer, R.K., Warkentin, E. and Ermler, U. Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O. FEBS J. 274 (2007) 1588–1599. [DOI] [PMID: 17480207]
[EC 1.5.3.22 created 2013]
 
 
EC 1.5.7.2     
Accepted name: coenzyme F420 oxidoreductase (ferredoxin)
Reaction: reduced coenzyme F420 + 2 oxidized ferredoxin = oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): Fd:F420 oxidoreductase; FpoF protein; ferredoxin:F420 oxidoreductase
Systematic name: coenzyme F420:ferredoxin oxidoreductase
Comments: The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Welte, C. and Deppenmeier, U. Re-evaluation of the function of the F420 dehydrogenase in electron transport of Methanosarcina mazei. FEBS J. 278 (2011) 1277–1287. [DOI] [PMID: 21306561]
[EC 1.5.7.2 created 2013]
 
 
EC 1.5.98.1     
Accepted name: methylenetetrahydromethanopterin dehydrogenase
Reaction: 5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
For diagram of methane biosynthesis, click here
Other name(s): N5,N10-methylenetetrahydromethanopterin dehydrogenase; 5,10-methylenetetrahydromethanopterin dehydrogenase
Systematic name: 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
Comments: Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in the methanogen Methanothermobacter thermautotrophicus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 100357-01-5
References:
1.  Hartzell, P.L., Zvilius, G., Escalante-Semerena, J.C. and Donnelly, M.I. Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 133 (1985) 884–890. [DOI] [PMID: 4084309]
2.  te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293–302. [DOI] [PMID: 1911853]
[EC 1.5.98.1 created 1989 as EC 1.5.99.9, modified 2004, transferred to EC 1.5.98.1 2014]
 
 
EC 1.5.98.2     
Accepted name: 5,10-methylenetetrahydromethanopterin reductase
Reaction: 5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
For diagram of methane biosynthesis, click here
Other name(s): 5,10-methylenetetrahydromethanopterin cyclohydrolase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
Systematic name: 5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase
Comments: Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaea.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
References:
1.  Ma, K. and Thauer, R.K. Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 191 (1990) 187–193. [DOI] [PMID: 2379499]
2.  te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293–302. [DOI] [PMID: 1911853]
3.  Ma, K. and Thauer, R.K. Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B. FEBS Lett. 268 (1990) 59–62. [DOI] [PMID: 1696553]
4.  te Brömmelstroet, B.W., Hensgens, C.M., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain ΔH*. J. Biol. Chem. 265 (1990) 1852–1857. [PMID: 2298726]
5.  te Brömmelstroet, B.W., Hensgens, C.M., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri. J. Bacteriol. 172 (1990) 564–571. [DOI] [PMID: 2298699]
[EC 1.5.98.2 created 2000 as EC 1.5.99.11, modified 2004, transferred to EC 1.5.98.2 2014]
 
 
EC 1.5.98.3     
Accepted name: coenzyme F420:methanophenazine dehydrogenase
Reaction: reduced coenzyme F420 + methanophenazine = oxidized coenzyme F420 + dihydromethanophenazine
Glossary: methanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}phenazine
dihydromethanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}-5,10-dihydrophenazine
Other name(s): F420H2 dehydrogenase; fpoBCDIF (gene names)
Systematic name: reduced coenzyme F420:methanophenazine oxidoreductase
Comments: The enzyme, found in some methanogenic archaea, is responsible for the reoxidation of coenzyme F420, which is reduced during methanogenesis, and for the reduction of methanophenazine to dihydromethanophenazine, which is required by EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. The enzyme is membrane-bound, and is coupled to proton translocation across the cytoplasmic membrane, generating a proton motive force that is used for ATP generation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brodersen, J., Gottschalk, G. and Deppenmeier, U. Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus volta. Arch. Microbiol. 171 (1999) 115–121. [PMID: 9914308]
2.  Baumer, S., Ide, T., Jacobi, C., Johann, A., Gottschalk, G. and Deppenmeier, U. The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases. J. Biol. Chem. 275 (2000) 17968–17973. [DOI] [PMID: 10751389]
3.  Deppenmeier, U. The membrane-bound electron transport system of Methanosarcina species. J. Bioenerg. Biomembr. 36 (2004) 55–64. [PMID: 15168610]
4.  Abken H. J. and Deppenmeier, U. Purification and properties of an F420H2 dehydrogenase from Methanosarcina mazei Gö1. FEMS Microbiol. Lett. 154 (2006) 231–237.
[EC 1.5.98.3 created 2017]
 
 
EC 1.8.98.3     
Accepted name: sulfite reductase (coenzyme F420)
Reaction: hydrogen sulfide + 3 oxidized coenzyme F420 + 3 H2O = sulfite + 3 reduced coenzyme F420
Other name(s): coenzyme F420-dependent sulfite reductase; Fsr
Systematic name: hydrogen sulfide:coenzyme F420 oxidoreductase
Comments: The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, is involved in sulfite detoxification and assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Johnson, E.F. and Mukhopadhyay, B. A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii. J. Biol. Chem. 280 (2005) 38776–38786. [DOI] [PMID: 16048999]
2.  Johnson, E.F. and Mukhopadhyay, B. Coenzyme F420-dependent sulfite reductase-enabled sulfite detoxification and use of sulfite as a sole sulfur source by Methanococcus maripaludis. Appl. Environ. Microbiol. 74 (2008) 3591–3595. [DOI] [PMID: 18378657]
[EC 1.8.98.3 created 2014]
 
 
EC 1.8.98.4     
Accepted name: coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase
Reaction: 2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
Glossary: CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine =
O3-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine
Other name(s): hdrA2B2C2 (gene names)
Systematic name: CoB,CoM,ferredoxin:coenzyme F420 oxidoreductase
Comments: The enzyme, characterized from the archaeon Methanosarcina acetivorans, catalyses the reduction of CoB-CoM heterodisulfide back to CoB and CoM. The enzyme consists of three components, HdrA, HdrB and HdrC, all of which contain [4Fe-4S] clusters. Electrons enter at HdrA, which also contains FAD, and are transferred via HdrC to the catalytic component, HdrB. During methanogenesis from acetate the enzyme catalyses the activity of EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase. However, it can also use electron bifurcation to direct electron pairs from reduced coenzyme F420 towards the reduction of both ferredoxin and CoB-CoM heterodisulfide. This activity is proposed to take place during Fe(III)-dependent anaerobic methane oxidation. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yan, Z., Wang, M. and Ferry, J.G. A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea. mBio 8 (2017) e02285-16. [DOI] [PMID: 28174314]
[EC 1.8.98.4 created 2017]
 
 
EC 1.12.98.1     
Accepted name: coenzyme F420 hydrogenase
Reaction: H2 + oxidized coenzyme F420 = reduced coenzyme F420
For diagram of reaction, click here
Glossary: coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
Other name(s): 8-hydroxy-5-deazaflavin-reducing hydrogenase; F420-reducing hydrogenase; coenzyme F420-dependent hydrogenase
Systematic name: hydrogen:coenzyme F420 oxidoreductase
Comments: An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methyl viologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-05-8
References:
1.  Adams, M.W.W., Mortenson, L.E. and Chen, J.-S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105–176. [PMID: 6786341]
2.  Yamazaki, S. A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue. J. Biol. Chem. 257 (1982) 7926–7929. [PMID: 6211447]
3.  Fox, J.A., Livingston, D.J., Orme-Johnson, W.H. and Walsh, C.T. 8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization. Biochemistry 26 (1987) 4219–4228. [PMID: 3663585]
4.  Muth, E., Morschel, E. and Klein, A. Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae. Eur. J. Biochem. 169 (1987) 571–577. [DOI] [PMID: 3121317]
5.  Baron, S.F. and Ferry, J.G. Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum. J. Bacteriol. 171 (1989) 3846–3853. [DOI] [PMID: 2738024]
[EC 1.12.98.1 created 1989 as EC 1.12.99.1, transferred 2002 to EC 1.12.98.1]
 
 
EC 1.17.98.3     
Accepted name: formate dehydrogenase (coenzyme F420)
Reaction: formate + oxidized coenzyme F420 = CO2 + reduced coenzyme F420
Other name(s): coenzyme F420 reducing formate dehydrogenase; coenzyme F420-dependent formate dehydrogenase
Systematic name: formate:coenzyme-F420 oxidoreductase
Comments: The enzyme, characterized from methanogenic archaea, is involved in formate-dependent H2 production. It contains noncovalently bound FAD [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schauer, N.L. and Ferry, J.G. FAD requirement for the reduction of coenzyme F420 by formate dehydrogenase from Methanobacterium formicicum. J. Bacteriol. 155 (1983) 467–472. [PMID: 6874636]
2.  Schauer, N.L. and Ferry, J.G. Composition of the coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum. J. Bacteriol. 165 (1986) 405–411. [DOI] [PMID: 3944055]
3.  Lupa, B., Hendrickson, E.L., Leigh, J.A. and Whitman, W.B. Formate-dependent H2 production by the mesophilic methanogen Methanococcus maripaludis. Appl. Environ. Microbiol. 74 (2008) 6584–6590. [DOI] [PMID: 18791018]
[EC 1.17.98.3 created 2014 as EC 1.2.99.9, transferred 2017 to EC 1.17.98.3]
 
 


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