The Enzyme Database

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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
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 1.6.5.12     
Accepted name: demethylphylloquinone reductase
Reaction: demethylphylloquinone + NADPH + H+ = demethylphylloquinol + NADP+
Glossary: demethylphylloquinone = 2-phytyl-1,4-naphthoquinone
Other name(s): ndbB (gene name); NDC1 (gene name); demethylphylloquinone:NADPH oxidoreductase
Systematic name: NADPH:demethylphylloquinone oxidoreductase
Comments: The enzyme, found in plants and cyanobacteria, is involved in the biosynthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme is a type II NADPH dehydrogenase and requires a flavine adenine dinucleotide cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fatihi, A., Latimer, S., Schmollinger, S., Block, A., Dussault, P.H., Vermaas, W.F., Merchant, S.S. and Basset, G.J. A dedicated type II NADPH dehydrogenase performs the penultimate step in the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis. Plant Cell 27 (2015) 1730–1741. [DOI] [PMID: 26023160]
[EC 1.6.5.12 created 2015]
 
 
EC 1.14.13.194      
Transferred entry: phylloquinone ω-hydroxylase. Now EC 1.14.14.78, phylloquinone ω-hydroxylase
[EC 1.14.13.194 created 2014, deleted 2018]
 
 
EC 1.14.14.78     
Accepted name: phylloquinone ω-hydroxylase
Reaction: phylloquinone + [reduced NADPH—hemoprotein reductase] + O2 = ω-hydroxyphylloquinone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of vitamin K biosynthesis, click here
Other name(s): vitamin K1 ω-hydroxylase; CYP4F2; CYP4F11
Systematic name: phylloquinone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxyphylloquinone-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from human tissue. The enzyme will also act on menaquinone-4. Prolonged action of CYP4F2, but not CYP4F11, on the ω hydroxyl group oxidizes it to the corresponding carboxylic acid. CYP4F2 also oxidizes leukotriene B4; see EC 1.14.13.30, leukotriene-B4 20-monooxygenase [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jin, R., Koop, D.R., Raucy, J.L. and Lasker, J.M. Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4. Arch. Biochem. Biophys. 359 (1998) 89–98. [DOI] [PMID: 9799565]
2.  Tang, Z., Salamanca-Pinzon, S.G., Wu, Z.L., Xiao, Y. and Guengerich, F.P. Human cytochrome P450 4F11: heterologous expression in bacteria, purification, and characterization of catalytic function. Arch. Biochem. Biophys. 494 (2010) 86–93. [DOI] [PMID: 19932081]
3.  Edson, K.Z., Prasad, B., Unadkat, J.D., Suhara, Y., Okano, T., Guengerich, F.P. and Rettie, A.E. Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. Biochemistry 52 (2013) 8276–8285. [DOI] [PMID: 24138531]
[EC 1.14.14.78 created 2014 as EC 1.14.13.194, transferred 2018 to EC 1.14.14.78]
 
 
EC 1.14.99.20     
Accepted name: phylloquinone monooxygenase (2,3-epoxidizing)
Reaction: phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
Other name(s): phylloquinone epoxidase; vitamin K 2,3-epoxidase; vitamin K epoxidase; vitamin K1 epoxidase
Systematic name: phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 54596-37-1
References:
1.  Willingham, A.K. and Matschiner, J.T. Changes in phylloquinone epoxidase activity related to prothrombin synthesis and microsomal clotting activity in the rat. Biochem. J. 140 (1974) 435–441. [PMID: 4155625]
[EC 1.14.99.20 created 1976]
 
 
EC 1.17.4.4     
Accepted name: vitamin-K-epoxide reductase (warfarin-sensitive)
Reaction: (1) phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues
(2) phylloquinol + a protein with a disulfide bond = phylloquinone + a protein with reduced L-cysteine residues
For diagram of the vitamin K cycle, click here
Glossary: phylloquinone = vitamin K1 = 2-methyl-3-phytyl-1,4-naphthoquinone
2,3-epoxyphylloquinone = vitamin K1 2,3-epoxide = 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone
Other name(s): VKORC1 (gene name); VKORC1L1 (gene name)
Systematic name: phylloquinone:disulfide oxidoreductase
Comments: The enzyme catalyses the reduction of vitamin K 2,3-epoxide, which is formed by the activity of EC 4.1.1.90, peptidyl-glutamate 4-carboxylase, back to its phylloquinol active form. The enzyme forms a tight complex with EC 5.3.4.1, protein disulfide-isomerase, which transfers the required electrons from newly-synthesized proteins by catalysing the formation of disulfide bridges. The enzyme acts on the epoxide forms of both phylloquinone (vitamin K1) and menaquinone (vitamin K2). Inhibited strongly by (S)-warfarin and ferulenol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55963-40-1
References:
1.  Whitlon, D.S., Sadowski, J.A. and Suttie, J.W. Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition. Biochemistry 17 (1978) 1371–1377. [PMID: 646989]
2.  Lee, J.L. and Fasco, M.J. Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction with a common disulfide. Biochemistry 23 (1984) 2246–2252. [PMID: 6733086]
3.  Mukharji, I. and Silverman, R.B. Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone. Proc. Natl. Acad. Sci. USA 82 (1985) 2713–2717. [DOI] [PMID: 3857611]
4.  Li, T., Chang, C.Y., Jin, D.Y., Lin, P.J., Khvorova, A. and Stafford, D.W. Identification of the gene for vitamin K epoxide reductase. Nature 427 (2004) 541–544. [PMID: 14765195]
5.  Wajih, N., Hutson, S.M. and Wallin, R. Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction. J. Biol. Chem. 282 (2007) 2626–2635. [PMID: 17124179]
6.  Spohn, G., Kleinridders, A., Wunderlich, F.T., Watzka, M., Zaucke, F., Blumbach, K., Geisen, C., Seifried, E., Muller, C., Paulsson, M., Bruning, J.C. and Oldenburg, J. VKORC1 deficiency in mice causes early postnatal lethality due to severe bleeding. Thromb Haemost 101 (2009) 1044–1050. [PMID: 19492146]
7.  Schulman, S., Wang, B., Li, W. and Rapoport, T.A. Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners. Proc. Natl. Acad. Sci. USA 107 (2010) 15027–15032. [PMID: 20696932]
[EC 1.17.4.4 created 1989 as EC 1.1.4.1, transferred 2014 to EC 1.17.4.4, modified 2018]
 
 
EC 1.97.1.12     
Accepted name: photosystem I
Reaction: reduced plastocyanin + oxidized ferredoxin + = oxidized plastocyanin + reduced ferredoxin
Systematic name: plastocyanin:ferredoxin oxidoreductase (light-dependent)
Comments: Contains chlorophyll, phylloquinones, carotenoids and [4Fe-4S] clusters. Cytochrome c6 can act as an alternative electron donor, and flavodoxin as an alternative acceptor in some species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Takabe, T., Iwasaki, Y., Hibino, T. and Ando, T. Subunit composition of photosystem I complex that catalyzes light-dependent transfer of electrons from plastocyanin to ferredoxin. J. Biochem. 110 (1991) 622–627. [PMID: 1778985]
2.  van Thor, J.J., Geerlings, T.H., Matthijs, H.C. and Hellingwerf, K.J. Kinetic evidence for the PsaE-dependent transient ternary complex photosystem I/Ferredoxin/Ferredoxin:NADP+ reductase in a cyanobacterium. Biochemistry 38 (1999) 12735–12746. [DOI] [PMID: 10504244]
3.  Chitnis, P.R. Photosystem I: function and physiology. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 593–626. [DOI] [PMID: 11337410]
4.  Amunts, A., Toporik, H., Borovikova, A. and Nelson, N. Structure determination and improved model of plant photosystem I. J. Biol. Chem. 285 (2010) 3478–3486. [DOI] [PMID: 19923216]
[EC 1.97.1.12 created 2011]
 
 
EC 2.1.1.329     
Accepted name: demethylphylloquinol methyltransferase
Reaction: S-adenosyl-L-methionine + demethylphylloquinol = S-adenosyl-L-homocysteine + phylloquinol
For diagram of vitamin K biosynthesis, click here
Glossary: demethylphylloquinol = 2-phytyl-1,4-naphthoquinol
phylloquinol = 2-methyl-3-phytyl-1,4-naphthoquinol = vitamin K1
Other name(s): menG (gene name); 2-phytyl-1,4-naphthoquinol methyltransferase
Systematic name: S-adenosyl-L-methionine:2-phytyl-1,4-naphthoquinol C-methyltransferase
Comments: The enzyme, found in plants and cyanobacteria, catalyses the final step in the biosynthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme is specific for the quinol form of the substrate, and does not act on the quinone form [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sakuragi, Y., Zybailov, B., Shen, G., Jones, A.D., Chitnis, P.R., van der Est, A., Bittl, R., Zech, S., Stehlik, D., Golbeck, J.H. and Bryant, D.A. Insertional inactivation of the menG gene, encoding 2-phytyl-1,4-naphthoquinone methyltransferase of Synechocystis sp. PCC 6803, results in the incorporation of 2-phytyl-1,4-naphthoquinone into the A1 site and alteration of the equilibrium constant between A1 and F(X) in photosystem I. Biochemistry 41 (2002) 394–405. [DOI] [PMID: 11772039]
2.  Lohmann, A., Schottler, M.A., Brehelin, C., Kessler, F., Bock, R., Cahoon, E.B. and Dormann, P. Deficiency in phylloquinone (vitamin K1) methylation affects prenyl quinone distribution, photosystem I abundance, and anthocyanin accumulation in the Arabidopsis AtmenG mutant. J. Biol. Chem. 281 (2006) 40461–40472. [DOI] [PMID: 17082184]
3.  Fatihi, A., Latimer, S., Schmollinger, S., Block, A., Dussault, P.H., Vermaas, W.F., Merchant, S.S. and Basset, G.J. A dedicated type II NADPH dehydrogenase performs the penultimate step in the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis. Plant Cell 27 (2015) 1730–1741. [DOI] [PMID: 26023160]
[EC 2.1.1.329 created 2016]
 
 
EC 2.5.1.130     
Accepted name: 2-carboxy-1,4-naphthoquinone phytyltransferase
Reaction: phytyl diphosphate + 2-carboxy-1,4-naphthoquinone = demethylphylloquinone + diphosphate + CO2
For diagram of vitamin K biosynthesis, click here
Glossary: 2-carboxy-1,4-naphthoquinone = 1,4-dioxo-2-naphthoic acid
Other name(s): menA (gene name); ABC4 (gene name); 1,4-dioxo-2-naphthoate phytyltransferase; 1,4-diketo-2-naphthoate phytyltransferase
Systematic name: phytyl-diphosphate:2-carboxy-1,4-naphthoquinone phytyltransferase
Comments: This enzyme, found in plants and cyanobacteria, catalyses a step in the synthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme catalyses the transfer of the phytyl chain synthesized by EC 1.3.1.83, geranylgeranyl diphosphate reductase, to 2-carboxy-1,4-naphthoquinone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Johnson, T.W., Shen, G., Zybailov, B., Kolling, D., Reategui, R., Beauparlant, S., Vassiliev, I.R., Bryant, D.A., Jones, A.D., Golbeck, J.H. and Chitnis, P.R. Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275 (2000) 8523–8530. [DOI] [PMID: 10722690]
2.  Shimada, H., Ohno, R., Shibata, M., Ikegami, I., Onai, K., Ohto, M.A. and Takamiya, K. Inactivation and deficiency of core proteins of photosystems I and II caused by genetical phylloquinone and plastoquinone deficiency but retained lamellar structure in a T-DNA mutant of Arabidopsis. Plant J. 41 (2005) 627–637. [DOI] [PMID: 15686525]
[EC 2.5.1.130 created 2015]
 
 
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
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]
[EC 3.1.2.28 created 2010]
 
 
EC 4.1.1.90     
Accepted name: peptidyl-glutamate 4-carboxylase
Reaction: peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinol
For diagram of the vitamin K cycle, click here
Other name(s): vitamin K-dependent carboxylase; γ-glutamyl carboxylase; peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing)
Systematic name: peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinol-epoxidizing)
Comments: The enzyme can use various vitamin-K derivatives, including menaquinol, but does not contain iron. The mechanism appears to involve the generation of a strong base by oxygenation of vitamin K. It catalyses the post-translational carboxylation of glutamate residues of several proteins of the blood-clotting system. 9–12 glutamate residues are converted to 4-carboxyglutamate (Gla) in a specific domain of the target protein. The 4-pro-S hydrogen of the glutamate residue is removed [5] and there is an inversion of stereochemistry at this position [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dowd, P., Hershline, R., Ham, S.W. and Naganathan, S. Vitamin K and energy transduction: a base strength amplification mechanism. Science 269 (1995) 1684–1691. [DOI] [PMID: 7569894]
2.  Furie, B., Bouchard, B.A. and Furie, B.C. Vitamin K-dependent biosynthesis of γ-carboxyglutamic acid. Blood 93 (1999) 1798–1808. [PMID: 10068650]
3.  Rishavy, M.A., Hallgren, K.W., Yakubenko, A.V., Shtofman, R.L., Runge, K.W. and Berkner, K.L. Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation. Biochemistry 45 (2006) 13239–13248. [DOI] [PMID: 17073445]
4.  Silva, P.J. and Ramos, M.J. Reaction mechanism of the vitamin K-dependent glutamate carboxylase: a computational study. J. Phys. Chem. B 111 (2007) 12883–12887. [DOI] [PMID: 17935315]
5.  Decottignies-Le Maréchal, P., Ducrocq, C., Marquet, A. and Azerad, R. The stereochemistry of hydrogen abstraction in vitamin K-dependent carboxylation. J. Biol. Chem. 259 (1984) 15010–15012. [PMID: 6150930]
6.  Dubois, J., Dugave, C., Foures, C., Kaminsky, M., Tabet, J.C., Bory, S., Gaudry, M. and Marquet, A. Vitamin K dependent carboxylation: determination of the stereochemical course using 4-fluoroglutamyl-containing substrate. Biochemistry 30 (1991) 10506–10512. [PMID: 1931973]
7.  Rishavy, M.A. and Berkner, K.L. Vitamin K oxygenation, glutamate carboxylation, and processivity: defining the three critical facets of catalysis by the vitamin K-dependent carboxylase. Adv Nutr 3 (2012) 135–148. [DOI] [PMID: 22516721]
[EC 4.1.1.90 created 2009, modified 2011]
 
 
EC 4.1.3.36     
Accepted name: 1,4-dihydroxy-2-naphthoyl-CoA synthase
Reaction: 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
For diagram of vitamin-K biosynthesis, click here
Other name(s): naphthoate synthase; 1,4-dihydroxy-2-naphthoate synthase; dihydroxynaphthoate synthase; o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing); MenB; o-succinylbenzoyl-CoA dehydratase (cyclizing)
Systematic name: 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA dehydratase (cyclizing)
Comments: This enzyme is involved in the synthesis of 1,4-dihydroxy-2-naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K2, in bacteria), phylloquinone (vitamin K1 in plants), and many plant pigments. The coenzyme A group is subsequently removed from the product by EC 3.1.2.28, 1,4-dihydroxy-2-naphthoyl-CoA hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61328-42-5
References:
1.  Meganathan, R. and Bentley, R. Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes. J. Bacteriol. 140 (1979) 92–98. [PMID: 500558]
2.  Kolkmann, R. and Leistner, E. 4-(2′-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis. Z. Naturforsch. C: Sci. 42 (1987) 1207–1214. [PMID: 2966501]
3.  Johnson, T.W., Shen, G., Zybailov, B., Kolling, D., Reategui, R., Beauparlant, S., Vassiliev, I.R., Bryant, D.A., Jones, A.D., Golbeck, J.H. and Chitnis, P.R. Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275 (2000) 8523–8530. [DOI] [PMID: 10722690]
4.  Truglio, J.J., Theis, K., Feng, Y., Gajda, R., Machutta, C., Tonge, P.J. and Kisker, C. Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. J. Biol. Chem. 278 (2003) 42352–42360. [DOI] [PMID: 12909628]
[EC 4.1.3.36 created 1992, modified 2010]
 
 


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