The Enzyme Database

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EC 1.2.99.2      
Transferred entry: carbon-monoxide dehydrogenase (acceptor). Now EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin)
[EC 1.2.99.2 created 1982, modified 1990, modified 2003, deleted 2016]
 
 
EC 1.5.7.1     
Accepted name: methylenetetrahydrofolate reductase (ferredoxin)
Reaction: 5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
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]
[EC 1.5.7.1 created 2005, modified 2021]
 
 
EC 1.7.99.4      
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)
[EC 1.7.99.4 created 1972, modified 1976, deleted 2017]
 
 
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]
[EC 1.9.6.1 created 1961]
 
 
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
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]
2.  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.
[EC 1.12.5.1 created 1999 as EC 1.12.99.3, transferred 2002 to EC 1.12.5.1]
 
 
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]
[EC 1.18.1.4 created 1984, modified 2001, modified 2011]
 
 
EC 1.20.99.1     
Accepted name: arsenate reductase (donor)
Reaction: arsenite + acceptor = arsenate + reduced acceptor
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]
2.  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]
[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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