EC
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1.2.99.2
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Transferred entry: | carbon-monoxide dehydrogenase (acceptor). Now EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin)
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[EC 1.2.99.2 created 1982, modified 1990, modified 2003, deleted 2016] |
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EC |
1.5.7.1 |
Accepted name: |
methylenetetrahydrofolate reductase (ferredoxin) |
Reaction: |
5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+ |
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For diagram of folate species interconversions, click here |
Other name(s): |
5,10-methylenetetrahydrofolate reductase |
Systematic name: |
5-methyltetrahydrofolate:ferredoxin oxidoreductase |
Comments: |
An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); or EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with either NADH or NADP+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Clark, J.E. and Ljungdahl, L.G. Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum. J. Biol. Chem. 259 (1984) 10845–10849. [PMID: 6381490] |
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[EC 1.5.7.1 created 2005, modified 2021] |
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EC
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1.7.99.4
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Transferred entry: | nitrate reductase, Now EC 1.7.1.1, nitrate reductase (NADH), EC 1.7.1.2, nitrate reductase [NAD(P)H], EC 1.7.1.3, nitrate reductase (NADPH), EC 1.7.5.1, nitrate reductase (quinone), EC 1.7.7.2, nitrate reductase (ferredoxin) and EC 1.9.6.1, nitrate reductase (cytochrome)
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[EC 1.7.99.4 created 1972, modified 1976, deleted 2017] |
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EC |
1.9.6.1 |
Accepted name: |
nitrate reductase (cytochrome) |
Reaction: |
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite |
Other name(s): |
respiratory nitrate reductase; benzyl viologen-nitrate reductase |
Systematic name: |
ferrocytochrome:nitrate oxidoreductase |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-42-9 |
References: |
1. |
Sadana, J.C. and McElroy, W.D. Nitrate reductase from Achromobacter fischeri. Purification and properties: function of flavins and cytochrome. Arch. Biochem. Biophys. 67 (1957) 16–34. [DOI] [PMID: 13412117] |
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[EC 1.9.6.1 created 1961] |
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EC |
1.12.5.1 |
Accepted name: |
hydrogen:quinone oxidoreductase |
Reaction: |
H2 + menaquinone = menaquinol |
Glossary: |
methyl viologen = 1,1′-dimethyl-4,4′-bipyridine-1,1′-diium
benzyl viologen = 1,1′-dibenzyl-4,4′-bipyridine-1,1′-diium
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Other name(s): |
hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase |
Systematic name: |
hydrogen:quinone oxidoreductase |
Comments: |
Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 151616-65-8 |
References: |
1. |
Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E. , Duchêne, A., Tripier, D., Juvenal, K. and Kröger, A. The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur. J. Biochem. 206 (1992) 93–102. [DOI] [PMID: 1587288] |
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Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E., Duchene, A., Tripier, D. and Juvenal, K. Erratum to "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes". Eur. J. Biochem. 214 (1993) 949–950. [DOI] [PMID: 8319698] |
3. |
Gross, R., Simon, J., Lancaster, C.R.D. and Kroger, A. Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H-2. Mol. Microbiol. 30 (1998) 639–646. [DOI] [PMID: 9822828] |
4. |
Bernhard, M., Benelli, B., Hochkoeppler, A., Zannoni, D. and Friedrich, B. Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16. Eur. J. Biochem. 248 (1997) 179–186. [DOI] [PMID: 9310376] |
5. |
Ferber, D.M. and Maier, R.J. Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase. FEMS Microbiol. Lett. 110 (1993) 257–264. [DOI] [PMID: 8354459] |
6. |
Ishii, M., Omori, T., Igarashi, Y., Adachi, O., Ameyama, M. and Kodama, T. Methionaquinone is a direct natural electron-acceptor for the membrane-bound hydrogenase in Hydrogenobacter thermophilus strain TK-6. Agric. Biol. Chem. 55 (1991) 3011–3016. |
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[EC 1.12.5.1 created 1999 as EC 1.12.99.3, transferred 2002 to EC 1.12.5.1] |
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EC |
1.18.1.4 |
Accepted name: |
rubredoxin—NAD(P)+ reductase |
Reaction: |
2 reduced rubredoxin + NAD(P)+ + H+ = 2 oxidized rubredoxin + NAD(P)H |
Glossary: |
benzyl viologen = 1,1′-dibenzyl-4,4′-bipyridinium
2,6-dichloroindophenol = 4-(2,6-dichloro-4-hydroxyphenylimino)cyclohexa-2,5-dien-1-one
menadione = 2-methyl-1,4-naphthoquinone
rubredoxin = iron-containing protein found in sulfur-metabolizing bacteria and archaea, participating in electron transfer |
Other name(s): |
rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase; rubredoxin-nicotinamide adenine; dinucleotide phosphate reductase; NAD(P)+-rubredoxin oxidoreductase; NAD(P)H-rubredoxin oxidoreductase |
Systematic name: |
rubredoxin:NAD(P)+ oxidoreductase |
Comments: |
The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80237-97-4 |
References: |
1. |
Petitdemange, H., Blusson, H. and Gay, R. Detection of NAD(P)H-rubredoxin oxidoreductases in Clostridia. Anal. Biochem. 116 (1981) 564–570. [DOI] [PMID: 6274224] |
2. |
Ma, K. and Adams, M.W.W. A hyperactive NAD(P)H:rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 181 (1999) 5530–5533. [PMID: 10464233] |
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[EC 1.18.1.4 created 1984, modified 2001, modified 2011] |
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EC |
1.20.99.1 |
Accepted name: |
arsenate reductase (donor) |
Reaction: |
arsenite + acceptor = arsenate + reduced acceptor |
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For diagram of arsenate catabolism, click here |
Other name(s): |
arsenate:(acceptor) oxidoreductase |
Systematic name: |
arsenate:acceptor oxidoreductase |
Comments: |
Benzyl viologen can act as an acceptor. Unlike EC 1.20.4.1, arsenate reductase (glutaredoxin), reduced glutaredoxin cannot serve as a reductant. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 146907-46-2 |
References: |
1. |
Krafft, T. and Macy, J.M. Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255 (1998) 647–653. [DOI] [PMID: 9738904] |
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Radabaugh, T.R. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase. Chem. Res. Toxicol. 13 (2000) 26–30. [DOI] [PMID: 10649963] |
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[EC 1.20.99.1 created 2000 as EC 1.97.1.6, transferred 2001 to EC 1.20.99.1] |
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