The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



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]
[EC 1.3.5.3 created 2010, modified 2020]
 
 
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]
[EC 1.3.99.18 created 1999]
 
 
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
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]
[EC 1.3.99.19 created 1999, modified 2006]
 
 
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-coenzyme 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 1.6.5.2     
Accepted name: NAD(P)H dehydrogenase (quinone)
Reaction: NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
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]
[EC 1.6.5.2 created 1961, transferred 1965 to EC 1.6.99.2, transferred 2005 to EC 1.6.5.2]
 
 
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, 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]
[EC 1.6.5.10 created 1972 as EC 1.6.99.6, transferred 2011 to EC 1.6.5.10]
 
 
EC 1.6.5.11      
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]
 
 
EC 1.6.99.3      
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]
 
 
EC 1.6.99.5      
Transferred entry: NADH dehydrogenase (quinone). Transferred to EC 1.6.5.11, NADH dehydrogenase (quinone)
[EC 1.6.99.5 created 1972, deleted 2014]
 
 
EC 1.6.99.6      
Transferred entry: NADPH dehydrogenase (quinone). Now EC 1.6.5.10, NADPH dehydrogenase (quinone)
[EC 1.6.99.6 created 1972, deleted 2011]
 
 
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, 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]
 
 


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