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
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1.14.99.27
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Transferred entry: | juglone 3-monooxygenase, now classified as EC 1.17.3.4, juglone 3-monooxygenase
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[EC 1.14.99.27 created 1989, deleted 2016] |
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EC |
1.17.3.4 |
Accepted name: |
juglone 3-hydroxylase |
Reaction: |
2 juglone + O2 = 2 3,5-dihydroxy-1,4-naphthoquinone (overall reaction) (1a) 2 juglone + 2 H2O = 2 naphthalene-1,2,4,8-tetrol (1b) 2 naphthalene-1,2,4,8-tetrol + O2 = 2 3,5-dihydroxy-1,4-naphthoquinone + 2 H2O |
Glossary: |
juglone = 5-hydroxy-1,4-naphthoquinone |
Other name(s): |
juglone hydroxylase; naphthoquinone hydroxylase; naphthoquinone-hydroxylase |
Systematic name: |
5-hydroxy-1,4-naphthoquinone,water:oxygen oxidoreductase (3-hydroxylating) |
Comments: |
Even though oxygen is consumed, molecular oxygen is not incorporated into the product. Catalysis starts by incorporation of an oxygen atom from a water molecule into the substrate. The naphthalene-1,2,4,8-tetrol intermediate is then oxidized by molecular oxygen, which is reduced to water. Also acts on 1,4-naphthoquinone, naphthazarin and 2-chloro-1,4-naphthoquinone. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 98865-54-4 |
References: |
1. |
Rettenmaier, H. and Lingens, F. Purification and some properties of two isofunctional juglone hydroxylases from Pseudomonas putida J1. Biol. Chem. Hoppe-Seyler 366 (1985) 637–646. [PMID: 4041238] |
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[EC 1.17.3.4 created 1989 as EC 1.14.99.27, transferred 2016 to EC 1.17.3.4] |
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EC |
3.1.2.28 |
Accepted name: |
1,4-dihydroxy-2-naphthoyl-CoA hydrolase |
Reaction: |
1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA |
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For diagram of vitamin K biosynthesis, click here |
Other name(s): |
menI (gene name); ydiL (gene name) |
Systematic name: |
1,4-dihydroxy-2-naphthoyl-CoA hydrolase |
Comments: |
This enzyme participates in the synthesis of menaquinones [4], phylloquinone [3], as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Muller, W. and Leistner, E. 1,4-Naphthoquinone, an intermediate in juglone (5-hydroxy-1,4-naphthoquinone) biosynthesis. Phytochemistry 15 (1976) 407–410. |
2. |
Eichinger, D., Bacher, A., Zenk, M.H. and Eisenreich, W. Quantitative assessment of metabolic flux by 13C NMR analysis. Biosynthesis of anthraquinones in Rubia tinctorum. J. Am. Chem. Soc. 121 (1999) 7469–7475. |
3. |
Widhalm, J.R., van Oostende, C., Furt, F. and Basset, G.J. A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. Proc. Natl. Acad. Sci. USA 106 (2009) 5599–5603. [DOI] [PMID: 19321747] |
4. |
Chen, M., Ma, X., Chen, X., Jiang, M., Song, H. and Guo, Z. Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. J. Bacteriol. 195 (2013) 2768–2775. [DOI] [PMID: 23564174] |
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[EC 3.1.2.28 created 2010] |
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EC |
5.2.1.8 |
Accepted name: |
peptidylprolyl isomerase |
Reaction: |
peptidylproline (ω=180) = peptidylproline (ω=0) |
Glossary: |
For definition of ω, click here |
Other name(s): |
PPIase; cyclophilin [misleading, see comments]; peptide bond isomerase; peptidyl-prolyl cis-trans isomerase |
Systematic name: |
peptidylproline cis-trans-isomerase |
Comments: |
The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95076-93-0 |
References: |
1. |
Fischer, G. and Bang, H. The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase. Biochim. Biophys. Acta 828 (1985) 39–42. [DOI] [PMID: 3882150] |
2. |
Fischer, G., Bang, H. and Mech, C. [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides] Biomed. Biochim. Acta 43 (1984) 1101–1111. [PMID: 6395866] |
3. |
Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. and Schmid, F.X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337 (1989) 476–478. [DOI] [PMID: 2492638] |
4. |
Takahashi, N., Hayano, T. and Suzuki, M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337 (1989) 473–475. [DOI] [PMID: 2644542] |
5. |
Hennig, L., Christner, C., Kipping, M., Schelbert, B., Rucknagel, K.P., Grabley, S., Kullertz, G. and Fischer, G. Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. Biochemistry 37 (1998) 5953–5960. [DOI] [PMID: 9558330] |
6. |
Fischer, G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33 (1994) 1415–1436. |
7. |
Harrison, R.K. and Stein, R.L. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry 29 (1990) 3813–3816. [PMID: 1693856] |
8. |
Eisenmesser, E.Z., Bosco, D.A., Akke, M. and Kern, D. Enzyme dynamics during catalysis. Science 295 (2002) 1520–1523. [DOI] [PMID: 11859194] |
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[EC 5.2.1.8 created 1989, modified 2002] |
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