EC |
1.3.5.3 |
Accepted name: |
protoporphyrinogen IX dehydrogenase (quinone) |
Reaction: |
protoporphyrinogen IX + 3 quinone = protoporphyrin IX + 3 quinol |
Other name(s): |
HemG; protoporphyrinogen IX dehydrogenase (menaquinone) |
Systematic name: |
protoporphyrinogen IX:quinone oxidoreductase |
Comments: |
Contains FMN. The enzyme participates in heme b biosynthesis. In the bacterium Escherichia coli it interacts with either ubiquinone or menaquinone, depending on whether the organism grows aerobically or anaerobically. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Boynton, T.O., Daugherty, L.E., Dailey, T.A. and Dailey, H.A. Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity. Biochemistry 48 (2009) 6705–6711. [DOI] [PMID: 19583219] |
2. |
Möbius, K., Arias-Cartin, R., Breckau, D., Hännig, A.L., Riedmann, K., Biedendieck, R., Schroder, S., Becher, D., Magalon, A., Moser, J., Jahn, M. and Jahn, D. Heme biosynthesis is coupled to electron transport chains for energy generation. Proc. Natl. Acad. Sci. USA 107 (2010) 10436–10441. [PMID: 20484676] |
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[EC 1.3.5.3 created 2010, modified 2020] |
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EC |
1.3.99.18 |
Accepted name: |
quinaldate 4-oxidoreductase |
Reaction: |
quinaldate + acceptor + H2O = kynurenate + reduced acceptor |
Other name(s): |
quinaldic acid 4-oxidoreductase |
Systematic name: |
quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating) |
Comments: |
The enzyme from Pseudomonas sp. AK2 also acts on quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize nicotinate; quinaldate is a substrate for both of these enzymes. 2,4,6-Trinitrobenzene sulfonate, 1,4-benzoquinone, 1,2-naphthoquinone, nitroblue tetrazolium, thionine and menadione will serve as an electron acceptor for the former enzyme and ferricyanide for the latter; Meldola blue, iodonitrotetrazolium chloride, phenazine methosulfate, 2,6-dichlorophenolindophenol and cytochrome c will act as electron acceptors for both. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 149885-77-8 |
References: |
1. |
Sauter, M., Tshisuaka, B., Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases. Biol. Chem. Hoppe Seyler 374 (1993) 1037–1046. [PMID: 8292263] |
2. |
Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol. Chem. Hoppe-Seyler 374 (1993) 363–376. [PMID: 8357532] |
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[EC 1.3.99.18 created 1999] |
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EC |
1.3.99.19 |
Accepted name: |
quinoline-4-carboxylate 2-oxidoreductase |
Reaction: |
quinoline-4-carboxylate + acceptor + H2O = 2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor |
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For diagram of reaction, click here |
Other name(s): |
quinaldic acid 4-oxidoreductase; quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating) |
Systematic name: |
quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating) |
Comments: |
A molybdenum—iron—sulfur flavoprotein with molybdopterin cytosine dinucleotide as the molybdenum cofactor. Quinoline, 4-methylquinoline and 4-chloroquinoline can also serve as substrates for the enzyme from Agrobacterium sp. 1B. Iodonitrotetrazolium chloride, thionine, menadione and 2,6-dichlorophenolindophenol can act as electron acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 175780-18-4 |
References: |
1. |
Bauer, G. and Lingens, F. Microbial metabolism of quinoline and related compounds. XV.
Quinoline-4-carboxylic acid oxidoreductase from Agrobacterium spec.1B: a
molybdenum-containing enzyme. Biol. Chem. Hoppe-Seyler 373 (1992) 699–705. [PMID: 1418685] |
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[EC 1.3.99.19 created 1999, modified 2006] |
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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 |
1.6.5.2 |
Accepted name: |
NAD(P)H dehydrogenase (quinone) |
Reaction: |
NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone |
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For diagram of the vitamin K cycle, click here |
Other name(s): |
menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD(P)H-quinone reductase; menadione oxidoreductase; NAD(P)H dehydrogenase; NAD(P)H menadione reductase; NAD(P)H-quinone dehydrogenase; NAD(P)H-quinone oxidoreductase; NAD(P)H: (quinone-acceptor)oxidoreductase; NAD(P)H: menadione oxidoreductase; NADH-menadione reductase; naphthoquinone reductase; p-benzoquinone reductase; reduced NAD(P)H dehydrogenase; viologen accepting pyridine nucleotide oxidoreductase; vitamin K reductase; diaphorase; reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase; vitamin-K reductase; NAD(P)H2 dehydrogenase (quinone); NQO1; QR1; NAD(P)H:(quinone-acceptor) oxidoreductase |
Systematic name: |
NAD(P)H:quinone oxidoreductase |
Comments: |
A flavoprotein. The enzyme catalyses a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone [6]. The animal, but not the plant, form of the enzyme is inhibited by dicoumarol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-20-6 |
References: |
1. |
di Prisco, G., Casola, L. and Giuditta, A. Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris. Biochem. J. 105 (1967) 455–460. [PMID: 4171422] |
2. |
Giuditta, A. and Strecker, H.J. Purification and some properties of a brain diaphorase. Biochim. Biophys. Acta 48 (1961) 10–19. [DOI] [PMID: 13705804] |
3. |
Märki, F. and Martius, C. Vitamin K-Reductase, Darsellung und Eigenschaften. Biochem. Z. 333 (1960) 111–135. [PMID: 13765127] |
4. |
Misaka, E. and Nakanishi, K. Studies on menadione reductase of bakers' yeast. I. Purification, crystallization and some properties. J. Biochem. (Tokyo) 53 (1963) 465–471. |
5. |
Wosilait, W.D. The reduction of vitamin K1 by an enzyme from dog liver. J. Biol. Chem. 235 (1960) 1196–1201. [PMID: 13846011] |
6. |
Sparla, F., Tedeschi, G. and Trost, P. NAD(P)H:(quinone-acceptor) oxidoreductase of tobacco leaves is a flavin mononucleotide-containing flavoenzyme. Plant Physiol. 112 (1996) 249–258. [PMID: 12226388] |
7. |
Braun, M., Bungert, S. and Friedrich, T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry 37 (1998) 1861–1867. [DOI] [PMID: 9485311] |
8. |
Jaiswal, A.K. Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases. Arch. Biochem. Biophys. 375 (2000) 62–68. [DOI] [PMID: 10683249] |
9. |
Li, R., Bianchet, M.A., Talalay, P. and Amzel, L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. USA 92 (1995) 8846–8850. [DOI] [PMID: 7568029] |
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[EC 1.6.5.2 created 1961, transferred 1965 to EC 1.6.99.2, transferred 2005 to EC 1.6.5.2] |
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EC |
1.6.5.10 |
Accepted name: |
NADPH dehydrogenase (quinone) |
Reaction: |
NADPH + H+ + a quinone = NADP+ + a quinol |
Other name(s): |
reduced nicotinamide adenine dinucleotide phosphate (quinone) dehydrogenase; NADPH oxidase; NADPH2 dehydrogenase (quinone) |
Systematic name: |
NADPH:(quinone-acceptor) oxidoreductase |
Comments: |
A flavoprotein [1, 2]. The enzyme from Escherichia coli is specific for NADPH and is most active with quinone derivatives and ferricyanide as electron acceptors [3].
Menaquinone can act as acceptor. The enzyme from hog liver is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-37-4 |
References: |
1. |
Koli, A.K., Yearby, C., Scott, W. and Donaldson, K.O. Purification and properties of three separate menadione reductases from hog liver. J. Biol. Chem. 244 (1969) 621–629. [PMID: 4388793] |
2. |
Hayashi, M., Hasegawa, K., Oguni, Y. and Unemoto, T. Characterization of FMN-dependent NADH-quinone reductase induced by menadione in Escherichia coli. Biochim. Biophys. Acta 1035 (1990) 230–236. [DOI] [PMID: 2118386] |
3. |
Hayashi, M., Ohzeki, H., Shimada, H. and Unemoto, T. NADPH-specific quinone reductase is induced by 2-methylene-4-butyrolactone in Escherichia coli. Biochim. Biophys. Acta 1273 (1996) 165–170. [DOI] [PMID: 8611590] |
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[EC 1.6.5.10 created 1972 as EC 1.6.99.6, transferred 2011 to EC 1.6.5.10] |
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EC
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1.6.5.11
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Deleted entry: | NADH dehydrogenase (quinone). Identical to EC 1.6.5.9, NADH:quinone reductase (non-electrogenic) |
[EC 1.6.5.11 created 1972 as EC 1.6.99.5, transferred 2015 to EC 1.6.5.11, deleted 2019] |
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EC
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1.6.99.3
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Deleted entry: | NADH dehydrogenase. The activity is covered by EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating) |
[EC 1.6.99.3 created 1961 as EC 1.6.2.1, transferred 1965 to EC 1.6.99.3, modified 2018, deleted 2020] |
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EC
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1.6.99.5
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Transferred entry: | NADH dehydrogenase (quinone). Transferred to EC 1.6.5.11, NADH dehydrogenase (quinone)
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[EC 1.6.99.5 created 1972, deleted 2014] |
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EC
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1.6.99.6
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Transferred entry: | NADPH dehydrogenase (quinone). Now EC 1.6.5.10, NADPH dehydrogenase (quinone)
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[EC 1.6.99.6 created 1972, deleted 2011] |
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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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