Continued from EC 1.5
Sections
EC 1.6.1 With NAD+ or NADP+ as acceptor
EC 1.6.2 With a heme protein as acceptor
EC 1.6.3 With oxygen as acceptor
EC 1.6.4 With a disulfide as acceptor
EC 1.6.5 With a quinone or similar compound as acceptor
EC 1.6.6 With a nitrogenous group as acceptor
EC 1.6.8 With a flavin as acceptor
EC 1.6.99 With other acceptors
Accepted name: NAD(P)+ transhydrogenase (Si-specific)
Reaction: NADPH + NAD+ = NADP+ + NADH
Other name(s): pyridine nucleotide transhydrogenase; transhydrogenase; NAD(P) transhydrogenase; nicotinamide adenine dinucleotide (phosphate) transhydrogenase; NAD transhydrogenase; NADH transhydrogenase; nicotinamide nucleotide transhydrogenase; NADPH-NAD transhydrogenase; pyridine nucleotide transferase; NADPH-NAD oxidoreductase; NADH-NADP-transhydrogenase; NADPH:NAD+ transhydrogenase; H+-Thase; non-energy-linked transhydrogenase; NAD(P) transhydrogenase (B-specific); NAD(P)+ transhydrogenase (B-specific); NADPH:NAD+ oxidoreductase (B-specific)
Systematic name: NADPH:NAD+ oxidoreductase (Si-specific)
Comments: The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It is Si-specific with respect to both NAD+ and NADP+. Also acts on deamino coenzymes [cf. EC 1.6.1.2 NAD(P)+ transhydrogenase (Re/Si-specific)].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9014-18-0
References:
1. Humphrey, G.F. The distribution and properties of transhydrogenase from animal tissues. Biochem. J. 65 (1957) 546-550.
2. You, K.-S. Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions. CRC Crit. Rev. Biochem. 17 (1985) 313-451. [PMID: 3157549]
Accepted name: NAD(P)+ transhydrogenase (Re/Si-specific)
Reaction: NADPH + NAD+ = NADP+ + NADH
Other name(s): pyridine nucleotide transhydrogenase; transhydrogenase; NAD(P) transhydrogenase; nicotinamide adenine dinucleotide (phosphate) transhydrogenase; NAD transhydrogenase; NADH transhydrogenase; nicotinamide nucleotide transhydrogenase; NADPH-NAD transhydrogenase; pyridine nucleotide transferase; NADPH-NAD oxidoreductase; NADH-NADP-transhydrogenase; NADPH:NAD+ transhydrogenase; H+-Thase; energy-linked transhydrogenase; NAD(P) transhydrogenase (AB-specific); NAD(P)+ transhydrogenase (AB-specific); NADPH:NAD+ oxidoreductase (AB-specific)
Systematic name: NADPH:NAD+ oxidoreductase (Re/Si-specific)
Comments: The enzyme from heart mitochondria is Re-specific with respect to NAD+ and Si-specific with respect to NADP+ [cf. EC 1.6.1.1 NAD(P)+ transhydrogenase (Si-specific)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-18-0 and 9072-60-0
References:
1. Fisher, R.R. and Earle, S.R. Membrane-bound pyridine dinucleotide transhydrogenases. In: Everse, J., Anderson, B. and You, K. (Eds.), The Pyridine Nucleotide Coenzymes, Academic Press, New York, 1982, p. 279-324.
2. You, K.-S. Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions. CRC Crit. Rev. Biochem. 17 (1985) 313-451. [PMID: 3157549]
Accepted name: cytochrome-b5 reductase
Reaction: NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
Other name(s): cytochrome b5 reductase; dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase; reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase; NADH-ferricytochrome b5 oxidoreductase; NADH-cytochrome b5 reductase; NADH 5α-reductase ; NADH-cytochrome-b5 reductase
Systematic name: NADH:ferricytochrome-b5 oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-25-1
References:
1. Mahler, H.R., Raw, I., Molinari, R. and do Amaral, D.F. Studies of electron transport enzymes. II. Isolation and some properties of a cytochrome-specific reduced diphosphopyridine nucleotide dehydrogenase from pig liver. J. Biol. Chem. 233 (1958) 230-239.
2. Strittmatter, P. Microsomal cytochrome b5 and cytochrome b5 reductase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 113-145.
3. Strittmatter, P. and Velick, S.F. The purification and properties of microsomal cytochrome reductase. J. Biol. Chem. 228 (1957) 785-799.
[EC 1.6.2.3 Deleted entry: cytochrome reductase (NADPH) (EC 1.6.2.3 created 1972, deleted 1965)]
Accepted name: NADPH—hemoprotein reductase
Reaction: NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
Other name(s): CPR; FAD-cytochrome c reductase; NADP—cytochrome c reductase; NADP—cytochrome reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase; NADPH:ferrihemoprotein oxidoreductase; NADPH—cytochrome P-450 oxidoreductase; NADPH—cytochrome c oxidoreductase; NADPH—cytochrome c reductase; NADPH—cytochrome p-450 reductase; NADPH—ferricytochrome c oxidoreductase; NADPH—ferrihemoprotein reductase; TPNH2 cytochrome c reductase; TPNH-cytochrome c reductase; aldehyde reductase (NADPH-dependent); cytochrome P-450 reductase; cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent); dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase; ferrihemoprotein P-450 reductase; reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase; reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
Systematic name: NADPH:hemoprotein oxidoreductase
Comments: A flavoprotein (FMN, FAD) containing both FMN and FAD. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. The enzyme catalyses the reduction of the heme-thiolate-dependent monooxygenases, such as EC 1.14.14.1, unspecific monooxygenase and reduction of EC 1.14.99.3, heme oxygenase (decyclizing). It is part of the microsomal hydroxylating system. It also reduces cytochrome b5 and cytochrome c.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-03-4
References:
1. Haas, E., Horecker, B.L. and Hogness, T.R. The enzymatic reduction of cytochrome c, cytochrome c reductase. J. Biol. Chem. 136 (1940) 747-774.
2. Horecker, B.L. Triphosphopyridine nucleotide-cytochrome c reductase in liver. J. Biol. Chem. 183, (1950) 593-605.
3. Lu, A.Y.H., Junk, K.W. and Coon, M.J. Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components. J. Biol. Chem. 244, (1969) 3714-3721. [PMID: 4389465]
4. Masters, B.S.S., Kamin, H., Gibson, Q.H. and Williams, C.H., Jr. Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 240, (1965) 921-931.
5. Williams, C.H.,Jr. and Kamin, H. Microsomal triphosphopyridine nucleotide-cytochrome c reductase in liver. J. Biol. Chem. 237, (1962) 587-595. p> 6.Masters, B.S.S., Bilimoria, M.H, Kamen, H. and Gibson, Q.H. The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase. J. Biol. Chem. 240, (1965) 4081-4088. [PMID: 4378860]
7. Sevrioukova, I.F. and Peterson, J.A. NADPH-P-450 reductase: Structural and functional comparisons of the eukaryotic and prokaryotic isoforms. Biochimie 77, (1995) 562-572. [PMID: 8589067]
8. Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S.S. and Kim, J.-J.P. Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes. Proc. Natl. Acad. Sci. USA 94, (1997) 8411-8416. [PMID: 9237990]
9. Munro, A.W., Noble, M.A., Robledo, L., Daff, S.N. and Chapman, S.K. Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry 40, (2001) 1956-1963. [PMID: 11329262]
10. Gutierrez, A., Grunau, A., Paine, M., Munro, A.W., Wolf, C.R., Roberts, G.C.K. and Scrutton, N.S. Electron transfer in human cytochrome P450 reductase. Biochem. Soc. Trans. 31, (2003) 497-501. [PMID: 12773143]
Accepted name: NADPH—cytochrome-c2 reductase
Reaction: NADPH + 2 ferricytochrome c2 = NADP+ + H+ + 2 ferrocytochrome c2
Other name(s): cytochrome c2 reductase (reduced nicotinamide adenine dinucleotide phosphate); cytochrome c2 reductase (reduced nicotinamide adinine dinucleotide phosphate, NADPH)
Systematic name: NADPH:ferricytochrome-c2 oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-32-9
References:
1. Sabo, D.J. and Orlando, J.A. Isolation, purification, and some properties of reduced nicotinamide adenine dinucleotide phosphate-cytochrome c2 reductase from Rhodopseudomonas spheroides. J. Biol. Chem. 243 (1968) 3742-3749. [PMID: 4385431]
Accepted name: leghemoglobin reductase
Reaction: NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
Other name(s): ferric leghemoglobin reductase
Systematic name: NAD(P)H:ferrileghemoglobin oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 60440-35-9
References:
1. Saari, L.L. and Klucas, R.V. Ferric leghemoglobin reductase from soybean root nodules. Arch. Biochem. Biophys. 231 (1984) 102-113. [PMID: 6539095]
Accepted name: NAD(P)H oxidase
Reaction: NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
Other name(s): THOX2; ThOX; dual oxidase; p138tox; thyroid NADPH oxidase; thyroid oxidase; thyroid oxidase 2; NADPH oxidase
Systematic name: NAD(P)H:oxygen oxidoreductase
Comments: Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 77106-92-4
References:
1. Moreno, J.C., Bikker, H., Kempers, M.J., van Trotsenburg, A.S., Baas, F., de Vijlder, J.J., Vulsma, T. and Ris-Stalpers, C. Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. N. Engl. J. Med. 347 (2002) 95-102. [PMID: 12110737]
2. De Deken, X., Wang, D., Dumont, J.E. and Miot, F. Characterization of ThOX proteins as components of the thyroid H2O2-generating system. Exp. Cell Res. 273 (2002) 187-196. [PMID: 11822874]
3. De Deken, X., Wang, D., Many, M.C., Costagliola, S., Libert, F., Vassart, G., Dumont, J.E. and Miot, F. Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J. Biol. Chem. 275 (2000) 23227-23233. [PMID: 10806195]
4. Dupuy, C., Ohayon, R., Valent, A., Noel-Hudson, M.S., Deme, D. and Virion, A Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs. J. Biol. Chem. 274 (1999) 37265-37269. [PMID: 10601291]
5. Leseney, A.M., Deme, D., Legue, O., Ohayon, R., Chanson, P., Sales, J.P., Pires de Carvalho, D., Dupuy, C. and Virion, A. Biochemical characterization of a Ca2+/NAD(P)H-dependent H2O2 generator in human thyroid tissue. Biochimie 81 (1999) 373-380. [PMID: 10401672]
6. Dupuy, C., Virion, A., Ohayon, R., Kaniewski, J., Deme, D. and Pommier, J. Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane. J. Biol. Chem. 266 (1991) 3739-3743. [PMID: 1995628]
[EC 1.6.4.2 Transferred entry: now EC 1.8.1.7, glutathione-disulfide reductase (EC 1.6.4.2 created 1961, modified 1989, deleted 2002)]
[EC 1.6.4.3 Transferred entry: now EC 1.8.1.4 dihydrolipoamide dehydrogenase (EC 1.6.4.3 created 1961, modified 1976, deleted 1983)]
[EC 1.6.4.4 Transferred entry: now EC 1.8.1.8, protein-disulfide reductase (EC 1.6.4.4 created 1965, deleted 2002)]
[EC 1.6.4.5 Transferred entry: now EC 1.8.1.9, thioredoxin-disulfide reductase (EC 1.6.4.5 created 1972, deleted 2002)]
[EC 1.6.4.6 Transferred entry: now EC 1.8.1.10, CoA-glutathione reductase (EC 1.6.4.6 created 1972, deleted 2002)]
[EC 1.6.4.7 Transferred entry: now EC 1.8.1.11, asparagusate reductase (EC 1.6.4.7 created 1978, deleted 2002)]
[EC 1.6.4.8 Transferred entry: now EC 1.8.1.12, trypanothione-disulfide reductase (EC 1.6.4.8 created 1989, deleted 2002)]
[EC 1.6.4.9 Transferred entry: now EC 1.8.1.13, bis-γ-glutamylcystine reductase (EC 1.6.4.9 created 1992, deleted 2002)]
[EC 1.6.4.10 Transferred entry: now EC 1.8.1.14, CoA-disulfide reductase (EC 1.6.4.10 created 1992, deleted 2002)]
EC 1.6.5.8 NADH:ubiquinone reductase (Na+-transporting)
EC 1.6.5.9 NADH:ubiquinone reductase (non-electrogenic)
EC 1.6.5.10 NADPH dehydrogenase (quinone)
Accepted name: NAD(P)H dehydrogenase (quinone)
Reaction: NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
For diagram of reaction 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. [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. [PMID: 9485311]
8. Jaiswal, A.K. Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases. Arch. Biochem. Biophys. 375 (2000) 62-68. [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. [PMID: 7568029]
Accepted name: NADH:ubiquinone reductase (H+-translocating)
Reaction: NADH + ubiquinone + 5 H+in = NAD+ + ubiquinol + 4 H+out
Other name(s): ubiquinone reductase; type 1 dehydrogenase; complex 1 dehydrogenase; coenzyme Q reductase; complex I (electron transport chain); complex I (mitochondrial electron transport); complex I (NADH:Q1 oxidoreductase); dihydronicotinamide adenine dinucleotide-coenzyme Q reductase; DPNH-coenzyme Q reductase; DPNH-ubiquinone reductase; mitochondrial electron transport complex 1; mitochondrial electron transport complex I; NADH coenzyme Q1 reductase; NADH-coenzyme Q oxidoreductase; NADH-coenzyme Q reductase; NADH-CoQ oxidoreductase; NADH-CoQ reductase; NADH-ubiquinone reductase; NADH-ubiquinone oxidoreductase; NADH-ubiquinone-1 reductase; reduced nicotinamide adenine dinucleotide-coenzyme Q reductase; NADH:ubiquinone oxidoreductase complex; NADH-Q6 oxidoreductase; electron transfer complex I; NADH2 dehydrogenase (ubiquinone)
Systematic name: NADH:ubiquinone oxidoreductase
Comments: A flavoprotein (FMN) containing iron-sulfur clusters. The complex is present in mitochondria and aerobic bacteria. Breakdown of the complex can release EC 1.6.99.3, NADH dehydrogenase. In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD+ to NADH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-04-0
References:
1. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd edn, vol. 4, Plenum Press, New York, 1985, pp. 1-70.
2. Herter, S.M., Kortluke, C.M. and Drews, G. Complex I of Rhodobacter capsulatus and its role in reverted electron transport. Arch. Microbiol. 169 (1998) 98-105. [PMID: 9446680]
3. Hunte, C., Zickermann, V. and Brandt, U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329 (2010) 448-451. [PMID: 20595580]
4. Efremov, R.G., Baradaran, R. and Sazanov, L.A. The architecture of respiratory complex I. Nature 465 (2010) 441-445. [PMID: 20505720]
Accepted name: monodehydroascorbate reductase (NADH)
Reaction: NADH + H+ + 2 monodehydroascorbate = NAD+ + 2 ascorbate
Other name(s): NADH:semidehydroascorbic acid oxidoreductase; MDHA; semidehydroascorbate reductase; AFR; AFR-reductase; ascorbic free radical reductase; ascorbate free radical reductase; SOR; MDAsA reductase (NADPH) ; SDA reductase; NADH:ascorbate radical oxidoreductase; NADH-semidehydroascorbate oxidoreductase; ascorbate free-radical reductase ; NADH:AFR oxidoreductase; monodehydroascorbate reductase (NADH2)
Systematic name: NADH:monodehydroascorbate oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-26-9
References:
1. Schulze, H.-U., Schott, H.-H. and Staudinger, H. Isolierung und Charakterisierung einer NADH: Semidehydroascorbinsäure-Oxidoreduktase aus Neurospora crassa. Hoppe-Seyler's Z. Physiol. Chem. 353 (1972) 1931-1942. [PMID: 4405497]
Accepted name: NADPH:quinone reductase
Reaction: NADPH + H+ + 2 quinone = NADP+ + 2 semiquinone
Other name(s): NADPH2:quinone reductase
Systematic name: NADPH:quinone oxidoreductase
Comments: A zinc enzyme, specific for NADPH. Catalyses the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates [1]. Dicoumarol [cf. EC 1.6.5.2 NAD(P)H dehydrogenase (quinone)] and nitrofurantoin are competitive inhibitors with respect to the quinone substrate. The semiquinone free radical product may be non-enzymically reduced to the hydroquinone or oxidized back to quinone in the presence of O2 [1]. In some mammals the enzyme is abundant in the lens of the eye, where it is identified with the protein ζ-crystallin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-20-6
References:
1. Rao, P.V., Krishna, C.M. and Zigler, J.S., Jr. Identification and characterization of the enzymatic activity of ζ-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase. J. Biol. Chem. 267 (1992) 96-102. [PMID: 1370456]
2. Duhaiman, A.S. Kinetic properties of camel lens ζ-crystallin. Int. J. Biochem. Cell Biol. 28 (1996) 1163-1168. [PMID: 8930141]
3. Bazzi, M.D. Interaction of camel lens ζ-crystallin with quinones: portrait of a substrate by fluorescence spectroscopy. Arch. Biochem. Biophys. 395 (2001) 185-190. [PMID: 11697855]
4. Tang, A. and Curthoys, N.P. Identification of ζ-crystallin/NADPH:quinone reductase as a renal glutaminase mRNA pH response element-binding protein. J. Biol. Chem. 276 (2001) 21375-21380. [PMID: 11294877]
Accepted name: p-benzoquinone reductase (NADPH)
Reaction: NADPH + H+ + p-benzoquinone = NADP+ + hydroquinone
For diagram of reaction click here.
Systematic name: NADPH:p-benzoquinone oxidoreductase
Comments: Involved in the 4-nitrophenol degradation pathway in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Spain, J.C. and Gibson, D.T. Pathway for bioremediation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57 (1991) 812-819.
Accepted name: 2-hydroxy-1,4-benzoquinone reductase
Reaction: 2-hydroxy-1,4-benzoquinone + NADH + H+ = 1,2,4-trihydroxybenzene + NAD+
For diagram of reaction click here.
Other name(s): hydroxybenzoquinone reductase; 1,2,4-trihydroxybenzene:NAD oxidoreductase; NADH:2-hydroxy-1,4-benzoquinone oxidoreductase
Systematic name: 2-hydroxy-1,4-benzoquinone:NADH oxidoreductase
Comments: A flavoprotein (FMN) that differs in substrate specificity from other quinone reductases. The enzyme in Burkholderia cepacia is inducible by 2,4,5-trichlorophenoxyacetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 214466-94-1
References:
1. Zaborina, O., Daubaras, D.L., Zago, A., Xun, L., Saido, K., Klem,T., Nikolic, D. and Chakrabarty, A.M. Novel pathway for conversion of chlorohydroxyquinol to maleylacetate in Burkholderia cepacia AC1100. J. Bacteriol. 180 (1998) 4667-4675. [PMID: 9721310]
Accepted name: NADH:ubiquinone reductase (Na+-transporting)
Reaction: NADH + H+ + ubiquinone + n Na+in = NAD+ + ubiquinol + n Na+out
Other name(s): Na+-translocating NADH-quinone reductase; (Na+-NQR)
Systematic name: NADH:ubiquinone oxidoreductase (Na+-translocating)
Comments: An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Beattie, P., Tan, K., Bourne, R.M., Leach, D., Rich, P.R. and Ward, F.B. Cloning and sequencing of four structural genes for the Na+-translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. FEBS Lett. 356 (1994) 333-338. [PMID: 7805867]
2. Nakayama, Y., Hayashi, M. and Unemoto, T. Identification of six subunits constituting Na+-translocating NADH-quinone reductase from the marine Vibrio alginolyticus. FEBS Lett. 422 (1998) 240-242. [PMID: 9490015]
3. Bogachev, A.V., Bertsova, Y.V., Barquera, B. and Verkhovsky, M.I. Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi. Biochemistry 40 (2001) 7318-7323. [PMID: 11401580]
4. Barquera, B., Hellwig, P., Zhou, W., Morgan, J.E., Hase, C.C., Gosink, K.K., Nilges, M., Bruesehoff, P.J., Roth, A., Lancaster, C.R. and Gennis, R.B. Purification and characterization of the recombinant Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry 41 (2002) 3781-3789. [PMID: 11888296]
5. Barquera, B., Nilges, M.J., Morgan, J.E., Ramirez-Silva, L., Zhou, W. and Gennis, R.B. Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. Biochemistry 43 (2004) 12322-12330. [PMID: 15379571]
Accepted name: NADH:ubiquinone reductase (non-electrogenic)
Reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol
Other name(s): ubiquinone reductase; coenzyme Q reductase; dihydronicotinamide adenine dinucleotide-coenzyme Q reductase; DPNH-coenzyme Q reductase; DPNH-ubiquinone reductase; NADH-coenzyme Q oxidoreductase; NADH-coenzyme Q reductase; NADH-CoQ oxidoreductase; NADH-CoQ reductase; NADH-ubiquinone reductase; NADH-ubiquinone oxidoreductase; reduced nicotinamide adenine dinucleotide-coenzyme Q reductase; NADH-Q6 oxidoreductase; electron transfer complex I; NADH2 dehydrogenase (ubiquinone)
Systematic name: NADH:ubiquinone oxidoreductase
Comments: A flavoprotein (FAD). Occurs in mitochondria of yeast and plants, and in aerobic bacteria. Has low activity with NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Moller, I.M, and Palmer, J.M. Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of plant mitochondria. Physiologia Plantarum 54 (1982) 267-274.
2. de Vries, S. and Grivell, L.A. Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem. 176 (1988) 377-384. [PMID: 3138118]
3. Kerscher, S.J., Okun, J.G. and Brandt, U. A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica. J. Cell Sci. 112 ( Pt 14) (1999) 2347-2354. [PMID: 10381390]
4. Rasmusson, A.G., Soole, K.L. and Elthon, T.E. Alternative NAD(P)H dehydrogenases of plant mitochondria. Annu. Rev. Plant Biol. 55 (2004) 23-39. [PMID: 15725055]
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:
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. [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. [PMID: 8611590]
[EC 1.6.6.2 Transferred entry: now EC 1.7.1.2, nitrate reductase [NAD(P)H] (EC 1.6.6.2 created 1961, deleted 2002)]
[EC 1.6.6.3 Transferred entry: now EC 1.7.1.3, nitrate reductase (NADPH) (EC 1.6.6.3 created 1961, deleted 2002)]
[EC 1.6.6.4 Transferred entry: now EC 1.7.1.4, nitrite reductase [NAD(P)H] (EC 1.6.6.4 created 1961, deleted 2002)]
[EC 1.6.6.5 Transferred entry: now EC 1.7.99.3 nitrite reductase (EC 1.6.6.5 created 1961, deleted 1964)]
[EC 1.6.6.6 Transferred entry: now EC 1.7.1.5, hyponitrite reductase (EC 1.6.6.6 created 1961, deleted 2002)]
[EC 1.6.6.7 Transferred entry: now EC 1.7.1.6, azobenzene reductase (EC 1.6.6.7 created 1961, deleted 2002)]
[EC 1.6.6.8 Transferred entry: now EC 1.7.1.7, GMP reductase (EC 1.6.6.8 created 1965, deleted 2002)]
Accepted name: trimethylamine-N-oxide reductase
Reaction: NADH + H+ + trimethylamine N-oxide = NAD+ + trimethylamine + H2O
Other name(s): trimethylamine N-oxide reductase; trimethylamine oxide reductase; TMAO reductase; TOR
Systematic name: NADH:trimethylamine-N-oxide oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37256-34-1
References:
1. Unemoto, T., Hayashi, M., Miyaki, K. and Hayashi, M. Intracellular localization and properties of trimethylamine-N-oxide reductase in Vibrio parahaemolyticus. Biochim. Biophys. Acta 110 (1965) 319-328. [PMID: 4286289]
[EC 1.6.6.10 Transferred entry: now EC 1.7.1.9, nitroquinoline-N-oxide reductase (EC 1.6.6.10 created 1972, deleted 2002)]
[EC 1.6.6.11 Transferred entry: now EC 1.7.1.10, hydroxylamine reductase (NADH) (EC 1.6.6.11 created 1972, deleted 2002)]
[EC 1.6.6.12 Transferred entry: now EC 1.7.1.11, 4-(dimethylamino)phenylazoxybenzene reductase (EC 1.6.6.12 created 1989, deleted 2002)]
[EC 1.6.6.13 Transferred entry: now EC 1.7.1.12, N-hydroxy-2-acetamidofluorene reductase (EC 1.6.6.13 created 1989, deleted 2002)]
[EC 1.6.7.1 Transferred entry: now EC 1.18.1.2 ferredoxin-NADP+ reductase (EC 1.6.7.1 created 1972, deleted 1978)]
[EC 1.6.7.2 Transferred entry: now EC 1.18.1.1 rubredoxin-NAD+ reductase (EC 1.6.7.2 created 1972, deleted 1978)]
[EC 1.6.8.2 Transferred entry: now EC 1.5.1.30, flavin reductase (EC 1.6.8.2 created 1982, deleted 2002)]
Accepted name: NADPH dehydrogenase
Reaction: NADPH + H+ + acceptor = NADP+ + reduced acceptor
Other name(s): NADPH2 diaphorase; NADPH diaphorase; OYE; diaphorase; dihydronicotinamide adenine dinucleotide phosphate dehydrogenase; NADPH-dehydrogenase; NADPH-diaphorase; NADPH2-dehydrogenase; old yellow enzyme; reduced nicotinamide adenine dinucleotide phosphate dehydrogenase; TPNH dehydrogenase; TPNH-diaphorase; triphosphopyridine diaphorase; triphosphopyridine nucleotide diaphorase; NADPH2 dehydrogenase; NADPH:(acceptor) oxidoreductase
Systematic name: NADPH:acceptor oxidoreductase
Comments: A flavoprotein (FMN in yeast, FAD in plants).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9001-68-7
References:
1. Åkesson, Å., Ehrenberg, A. and Theorell, H. Old yellow enzyme. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 477-494.
2. Avron, M. and Jagendorf, A.T. Some further investigations on chloroplast TPNH diaphorase. Arch. Biochem. Biophys. 72 (1957) 17-24.
3. Jagendorf, A.T. Chloroplast TPNH diaphorase. Methods Enzymol. 6 (1963) 430-434.
4. Theorell, H. Das gelbe Oxydationsferment. Biochem. Z. 278 (1935) 263-290.
5. Theorell, H. and Åkesson, Å. Molecular weight and FMN content of crystalline "old yellow enzyme". Arch. Biochem. Biophys. 65 (1956) 439-448.
[EC 1.6.99.2 Transferred entry: now EC 1.6.5.2, NAD(P)H dehydrogenase (quinone). The enzyme was erroneously transferred from this sub-subclass in 1965 (EC 1.6.99.2 created 1961 as EC 1.6.5.2, transferred 1965 to EC 1.6.99.2, deleted 2005)]
Accepted name: NADH dehydrogenase
Reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor
Other name(s): cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH:(acceptor) oxidoreductase
Systematic name: NADH:acceptor oxidoreductase
Comments: A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Formerly EC 1.6.2.1; present in a mitochondrial complex as EC 1.6.5.3 NADH dehydrogenase (ubiquinone).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9079-67-8
References:
1. Adachi, K. and Okuyama, T. Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. Biochim. Biophys. Acta 268 (1972) 629-637. [PMID: 4402556]
2. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A.N. (Ed.), The Enzymes of Biological Membranes, 2nd ed., vol. 4, Wiley, New York, 1985, p. 1-70.
3. Hochstein, L.I. and Dalton, B.P. Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme. Biochim. Biophys. Acta 302 (1973) 216-228. [PMID: 4144655]
4. Kaniuga, Z. The transformation of mitochondrial NADH dehydrogenase into NADH:Cytochrome c oxidoreductase. Biochim. Biophys. Acta 73 (1963) 550-564.
[EC 1.6.99.4 Transferred entry: now EC 1.18.1.2 ferredoxin-NADP+ reductase (EC 1.6.99.4 created 1965, deleted 1972)]
Accepted name: NADH dehydrogenase (quinone)
Reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor
Other name(s): reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase; NADH-quinone oxidoreductase; DPNH-menadione reductase; D-diaphorase; NADH2 dehydrogenase (quinone)
Systematic name: NADH:(quinone-acceptor) oxidoreductase
Comments: Menaquinone can act as acceptor. Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-36-3
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]
[EC 1.6.99.6 Transferred entry: Transferred to EC 1.6.5.10, NADPH dehydrogenase (quinone) (EC 1.6.99.6 created 1972, deleted 2011)]
[EC 1.6.99.7 Transferred entry: now EC 1.5.1.34 6,7-dihydropteridine reductase. (EC 1.6.99.7 created 1972, modified 1981 (EC 1.6.99.10 created 1978, incorporated 1981), deleted 2003)]
[EC 1.6.99.8 Transferred entry: now EC 1.16.1.3, aquacobalamin reductase (EC 1.6.99.8 created 1972, deleted 2002)]
[EC 1.6.99.9 Transferred entry: now EC 1.16.1.4, cob(II)alamin reductase (EC 1.6.99.9 created 1972, deleted 2002)]
EC 1.6.99.10 Deleted entry: now included with EC 1.5.1.34, 6,7-dihydropteridine reductase [EC 1.6.99.10 created 1978, deleted 1981]
[EC 1.6.99.11 Transferred entry: now EC 1.16.1.5, aquacobalamin reductase (NADPH) (EC 1.6.99.11 created 1989, deleted 2002)]
[EC 1.6.99.12 Transferred entry: now EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating) (EC 1.6.99.12 created 1989, deleted 2002)]
[EC 1.6.99.13 Transferred entry: now EC 1.16.1.7, ferric-chelate reductase (EC 1.6.99.13 created 1992, deleted 2002)]