The Enzyme Database

Displaying entries 51-100 of 695.

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EC 1.7.5.2     
Accepted name: nitric oxide reductase (menaquinol)
Reaction: 2 nitric oxide + menaquinol = nitrous oxide + menaquinone + H2O
Comments: Contains copper.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cramm, R., Pohlmann, A. and Friedrich, B. Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16. FEBS Lett. 460 (1999) 6–10. [DOI] [PMID: 10571051]
2.  Suharti, Strampraad, M.J., Schroder, I. and de Vries, S. A novel copper A containing menaquinol NO reductase from Bacillus azotoformans. Biochemistry 40 (2001) 2632–2639. [DOI] [PMID: 11327887]
3.  Suharti, Heering, H.A. and de Vries, S. NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551. Biochemistry 43 (2004) 13487–13495. [DOI] [PMID: 15491156]
[EC 1.7.5.2 created 2011]
 
 
EC 1.7.7.1     
Accepted name: ferredoxin—nitrite reductase
Reaction: NH3 + 2 H2O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H+
Systematic name: ammonia:ferredoxin oxidoreductase
Comments: An iron protein. Contains siroheme and [4Fe-4S] clusters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-44-3
References:
1.  Joy, K.W. and Hageman, R.H. The purification and properties of nitrite reductase from higher plants, and its dependence on ferredoxin. Biochem. J. 100 (1966) 263–273. [PMID: 4381617]
2.  Ramirez, J.M., Del Campo, F.F., Paneque, A. and Losada, M. Ferredoxin-nitrite reductase from spinach. Biochim. Biophys. Acta 118 (1966) 58–71. [PMID: 5954064]
3.  Zumft, W.G., Paneque, A., Aparicio, P.J. and Losada, M. Mechanism of nitrate reduction in Chlorella. Biochem. Biophys. Res. Commun. 36 (1969) 980–986. [DOI] [PMID: 4390523]
[EC 1.7.7.1 created 1972, modified 1999]
 
 
EC 1.8.2.2     
Accepted name: thiosulfate dehydrogenase
Reaction: 2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c
Other name(s): tsdA (gene name); tetrathionate synthase; thiosulfate oxidase; thiosulfate-oxidizing enzyme; thiosulfate-acceptor oxidoreductase
Systematic name: thiosulfate:ferricytochrome-c oxidoreductase
Comments: The enzyme catalyses the reversible formation of a sulfur-sulfur bond between the sulfane atoms of two thiosulfate molecules, yielding tetrathionate and releasing two electrons. In many bacterial species the enzyme is a diheme c-type cytochrome. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, a second diheme cytochrome (TsdB) acts as the electron acceptor. However, some organisms, such as Allochromatium vinosum, lack TsdB. The electron acceptor in these organisms may be the high-potential iron-sulfur protein (HiPIP).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-88-4
References:
1.  Lu, W.-P. and Kelly, D.P. Cellular location and partial purification of the 'thiosulphate-oxidizing enzyme' and 'trithionate hydrolase' from Thiobacillus tepidarius. J. Gen. Microbiol. 134 (1988) 877–885.
2.  Fukumori, Y. and Yamanaka, T. A high-potential nonheme iron protein (HiPIP)-linked, thiosulfate-oxidizing enzyme derived from Chromatium vinosum. Curr. Microbiol. 3 (1979) 117–120.
3.  Liu, Y.W., Denkmann, K., Kosciow, K., Dahl, C. and Kelly, D.J. Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria. Mol. Microbiol. 88 (2013) 173–188. [DOI] [PMID: 23421726]
4.  Brito, J.A., Denkmann, K., Pereira, I.A., Archer, M. and Dahl, C. Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum: structural and functional insights into thiosulfate oxidation. J. Biol. Chem. 290 (2015) 9222–9238. [DOI] [PMID: 25673691]
5.  Kurth, J.M., Brito, J.A., Reuter, J., Flegler, A., Koch, T., Franke, T., Klein, E.M., Rowe, S.F., Butt, J.N., Denkmann, K., Pereira, I.A., Archer, M. and Dahl, C. Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase. J. Biol. Chem. 291 (2016) 24804–24818. [DOI] [PMID: 27694441]
[EC 1.8.2.2 created 1990]
 
 
EC 1.8.2.5     
Accepted name: thiosulfate reductase (cytochrome)
Reaction: sulfite + hydrogen sulfide + 2 ferricytochrome c3 = thiosulfate + 2 ferrocytochrome c3
Systematic name: sulfite,hydrogen sulfide:ferricytochrome-c3 oxidoreductase (thiosulfate-forming)
Comments: The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 1.12.2.1, cytochrome-c3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 1.8.99.5, dissimilatory sulfite reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ishimoto, M. and Koyama, J. On the role of a cytochrome in the thiosulfate reduction by sulfate-reducing bacterium. B. Chem. Soc. Jpn. 28 (1955) 231b–232.
2.  Ishimoto, M., Toyama, J. Biochemical studies on sulfate reducing bacteria. VI. Separation of hydrogenase and thiosulfate reductase and partial purification of cytochrome and green pigment. J. Biochem. (Tokyo) 44 (1957) 233–242.
3.  Nakatsukasa, W. and Akagi, J.M. Thiosulfate reductase isolated from Desulfotomaculum nigrificans. J. Bacteriol. 98 (1969) 429–433. [PMID: 5784203]
4.  Haschke, R.H. and Campbell, L.L. Thiosulfate reductase of Desulfovibrio vulgaris. J. Bacteriol. 106 (1971) 603–607. [PMID: 5573735]
5.  Hatchikian, E.C. Purification and properties of thiosulfate reductase from Desulfovibrio gigas. Arch. Microbiol. 105 (1975) 249–256. [PMID: 242299]
6.  Aketagawa, J., Kobayashi, K. and Ishimoto, M. Purification and properties of thiosulfate reductase from Desulfovibrio vulgaris, Miyazaki F. J. Biochem. 97 (1985) 1025–1032. [PMID: 2993256]
[EC 1.8.2.5 created 2017]
 
 
EC 1.8.4.8     
Accepted name: phosphoadenylyl-sulfate reductase (thioredoxin)
Reaction: adenosine 3′,5′-bisphosphate + sulfite + thioredoxin disulfide = 3′-phosphoadenylyl sulfate + thioredoxin
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): PAPS reductase, thioredoxin-dependent; PAPS reductase; thioredoxin:adenosine 3′-phosphate 5′-phosphosulfate reductase; 3′-phosphoadenylylsulfate reductase; thioredoxin:3′-phospho-adenylylsulfate reductase; phosphoadenosine-phosphosulfate reductase; adenosine 3′,5′-bisphosphate,sulfite:oxidized-thioredoxin oxidoreductase (3′-phosphoadenosine-5′-phosphosulfate-forming)
Systematic name: adenosine 3′,5′-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3′-phosphoadenosine-5′-phosphosulfate-forming)
Comments: Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-63-7
References:
1.  Berendt, U., Haverkamp, T., Prior, A., Schwenn, J.D. Reaction mechanism of thioredoxin: 3′-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 (1995) 347–356. [DOI] [PMID: 7588765]
[EC 1.8.4.8 created 1999 as EC 1.8.99.4, transferred 2000 to EC 1.8.4.8]
 
 
EC 1.8.4.9     
Accepted name: adenylyl-sulfate reductase (glutathione)
Reaction: AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione
Other name(s): 5′-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5′-phosphosulfate-forming); plant-type 5′-adenylylsulfate reductase
Systematic name: AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5′-phosphosulfate-forming)
Comments: This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase, in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or 2-sulfanylethan-1-ol (2-mercaptoethanol). The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Ulva intestinalis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 355840-27-6
References:
1.  Gutierrez-Marcos, J.F., Roberts, M.A., Campbell, E.I. and Wray, J.L. Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and 'APS reductase' activity. Proc. Natl. Acad. Sci. USA 93 (1996) 13377–13382. [DOI] [PMID: 8917599]
2.  Setya, A., Murillo, M. and Leustek, T. Sulfate reduction in higher plants: Molecular evidence for a novel 5-adenylylphosphosulfate (APS) reductase. Proc. Natl. Acad. Sci. USA 93 (1996) 13383–13388. [DOI] [PMID: 8917600]
3.  Bick, J.A., Aslund, F., Cen, Y. and Leustek, T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5′-adenylylsulfate reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 8404–8409. [DOI] [PMID: 9653199]
[EC 1.8.4.9 created 2000, modified 2002]
 
 
EC 1.8.4.10     
Accepted name: adenylyl-sulfate reductase (thioredoxin)
Reaction: AMP + sulfite + thioredoxin disulfide = 5′-adenylyl sulfate + thioredoxin
Other name(s): thioredoxin-dependent 5′-adenylylsulfate reductase
Systematic name: AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5′-phosphosulfate-forming)
Comments: Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin). Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate reductase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bick, J.A., Dennis, J.J., Zylstra, G.J., Nowack, J. and Leustek, T. Identification of a new class of 5-adenylylsulfate (APS) reductase from sulfate-assimilating bacteria. J. Bacteriol. 182 (2000) 135–142. [DOI] [PMID: 10613872]
2.  Abola, A.P., Willits, M.G., Wang, R.C. and Long, S.R. Reduction of adenosine-5′-phosphosulfate instead of 3′-phosphoadenosine-5′-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae. J. Bacteriol. 181 (1999) 5280–5287. [PMID: 10464198]
3.  Williams, S.J., Senaratne, R.H., Mougous, J.D., Riley, L.W. and Bertozzi, C.R. 5′-Adenosinephosphosulfate lies at a metabolic branchpoint in mycobacteria. J. Biol. Chem. 277 (2002) 32606–32615. [DOI] [PMID: 12072441]
4.  Neumann, S., Wynen, A., Truper, H.G. and Dahl, C. Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway. Mol. Biol. Rep. 27 (2000) 27–33. [PMID: 10939523]
[EC 1.8.4.10 created 2003]
 
 
EC 1.8.99.2     
Accepted name: adenylyl-sulfate reductase
Reaction: AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
Other name(s): adenosine phosphosulfate reductase; adenosine 5′-phosphosulfate reductase; APS-reductase; APS reductase; AMP, sulfite:(acceptor) oxidoreductase (adenosine-5′-phosphosulfate-forming)
Systematic name: AMP,sulfite:acceptor oxidoreductase (adenosine-5′-phosphosulfate-forming)
Comments: An iron flavoprotein (FAD). Methyl viologen can act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-75-2
References:
1.  Michaels, G.B., Davidson, J.T. and Peck, H.D., Jr. A flavin-sulfite adduct as an intermediate in the reaction catalyzed by adenylyl sulfate reductase from Desulfovibrio vulgaris. Biochem. Biophys. Res. Commun. 39 (1970) 321–328. [DOI] [PMID: 5421934]
[EC 1.8.99.2 created 1972]
 
 
EC 1.10.3.10      
Transferred entry: ubiquinol oxidase (H+-transporting). Now EC 7.1.1.3, ubiquinol oxidase (H+-transporting)
[EC 1.10.3.10 created 2011, modified 2014, deleted 2018]
 
 
EC 1.11.1.10     
Accepted name: chloride peroxidase
Reaction: RH + chloride + H2O2 = RCl + 2 H2O
Other name(s): chloroperoxidase; CPO; vanadium haloperoxidase
Systematic name: chloride:hydrogen-peroxide oxidoreductase
Comments: Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9055-20-3
References:
1.  Morris, D.R. and Hager, L.P. Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein. J. Biol. Chem. 241 (1966) 1763–1768. [PMID: 5949836]
2.  Hager, L.P., Hollenberg, P.F., Rand-Meir, T., Chiang, R. and Doubek, D.L. Chemistry of peroxidase intermediates. Ann. N.Y. Acad. Sci. 244 (1975) 80–93. [DOI] [PMID: 1056179]
3.  Theiler, R., Cook, J.C., Hager, L.P. and Siuda, J.F. Halohydrocarbon synthesis by bromoperoxidase. Science 202 (1978) 1094–1096. [DOI] [PMID: 17777960]
4.  Sundaramoorthy, M., Terner, J. and Poulos, T.L. The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid. Structure 3 (1995) 1367–1377. [DOI] [PMID: 8747463]
5.  ten Brink, H.B., Tuynman, A., Dekker, H.L., Hemrika, W., Izumi, Y., Oshiro, T., Schoemaker, H.E. and Wever, R. Enantioselective sulfoxidation catalyzed by vanadium haloperoxidases. Inorg. Chem. 37 (1998) 6780–6784. [DOI] [PMID: 11670813]
6.  ten Brink, H.B., Dekker, H.L., Schoemaker, H.E. and Wever, R. Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis. J. Inorg. Biochem. 80 (2000) 91–98. [DOI] [PMID: 10885468]
7.  Manoj, K.M. Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process. Biochim. Biophys. Acta 1764 (2006) 1325–1339. [DOI] [PMID: 16870515]
8.  Kuhnel, K., Blankenfeldt, W., Terner, J. and Schlichting, I. Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J. Biol. Chem. 281 (2006) 23990–23998. [DOI] [PMID: 16790441]
9.  Manoj, K.M. and Hager, L.P. Chloroperoxidase, a janus enzyme. Biochemistry 47 (2008) 2997–3003. [DOI] [PMID: 18220360]
[EC 1.11.1.10 created 1972, modified 2011]
 
 
EC 1.12.2.1     
Accepted name: cytochrome-c3 hydrogenase
Reaction: H2 + 2 ferricytochrome c3 = 2 H+ + 2 ferrocytochrome c3
Other name(s): H2:ferricytochrome c3 oxidoreductase; cytochrome c3 reductase; cytochrome hydrogenase; hydrogenase [ambiguous]
Systematic name: hydrogen:ferricytochrome-c3 oxidoreductase
Comments: An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-05-8
References:
1.  DerVartanian, D.V. and Le Gall, J. A monomolecular electron transfer chain: structure and function of cytochrome c3. Biochim. Biophys. Acta 346 (1974) 79–99. [PMID: 4364940]
2.  Higuchi, Y., Yasuoka, N., Kakudo, M., Katsube, Y., Yagi, T. and Inokuchi, H. Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Chem. 262 (1987) 2823–2825. [PMID: 3546297]
3.  Rilkis, E. and Rittenberg, D. Some observations on the enzyme, hydrogenase. J. Biol. Chem. 236 (1961) 2526–2529. [PMID: 13741672]
4.  Sadana, J.C. and Morey, A.V. Purification and properties of the hydrogenase of Desulfovibrio desulfuricans. Biochim. Biophys. Acta 50 (1961) 153–163. [DOI] [PMID: 13745271]
5.  Volbeda, A., Charon, M.H., Piras, C., Hatchikian, E.C., Frey, M. and Fontecillacamps, J.C. Crystal-structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 373 (1995) 580–587. [DOI] [PMID: 7854413]
6.  Garcin, E., Vernede, X., Hatchikian, E.C., Volbeda, A., Frey, M. and Fontecilla-Camps, J.C. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 7 (1999) 557–566. [DOI] [PMID: 10378275]
[EC 1.12.2.1 created 1972, modified 2002]
 
 
EC 1.13.11.63     
Accepted name: β-carotene 15,15′-dioxygenase
Reaction: β-carotene + O2 = 2 all-trans-retinal
For diagram of retinal and derivatives biosynthesis, click here
Other name(s): blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15′-dioxygenase; BCMO1 (misleading); β-carotene 15,15′-monooxygenase (incorrect)
Systematic name: β-carotene:oxygen 15,15′-dioxygenase (bond-cleaving)
Comments: Requires Fe2+. The enzyme cleaves β-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process β-cryptoxanthin, 8′-apo-β-carotenal, 4′-apo-β-carotenal, α-carotene and γ-carotene in decreasing order. The presence of at least one unsubstituted β-ionone ring in a substrate greater than C30 is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Goodman, D.S., Huang, H.S. and Shiratori, T. Mechanism of the biosynthesis of vitamin A from β-carotene. J. Biol. Chem. 241 (1966) 1929–1932. [PMID: 5946623]
2.  Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 242 (1967) 3543–3554.
3.  Yan, W., Jang, G.F., Haeseleer, F., Esumi, N., Chang, J., Kerrigan, M., Campochiaro, M., Campochiaro, P., Palczewski, K. and Zack, D.J. Cloning and characterization of a human β,β-carotene-15,15′-dioxygenase that is highly expressed in the retinal pigment epithelium. Genomics 72 (2001) 193–202. [DOI] [PMID: 11401432]
4.  Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal. Angew. Chem. 40 (2001) 2614–2616. [DOI] [PMID: 11458349]
5.  Kim, Y.S. and Oh, D.K. Substrate specificity of a recombinant chicken β-carotene 15,15′-monooxygenase that converts β-carotene into retinal. Biotechnol. Lett. 31 (2009) 403–408. [DOI] [PMID: 18979213]
6.  Kim, Y.S., Kim, N.H., Yeom, S.J., Kim, S.W. and Oh, D.K. In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a β-carotene 15,15′-dioxygenase. J. Biol. Chem. 284 (2009) 15781–15793. [DOI] [PMID: 19366683]
7.  Kim, Y.S., Park, C.S. and Oh, D.K. Retinal production from β-carotene by β-carotene 15,15′-dioxygenase from an unculturable marine bacterium. Biotechnol. Lett. 32 (2010) 957–961. [DOI] [PMID: 20229064]
8.  dela Seña, C., Riedl, K.M., Narayanasamy, S., Curley, R.W., Jr., Schwartz, S.J. and Harrison, E.H. The human enzyme that converts dietary provitamin A carotenoids to vitamin A is a dioxygenase. J. Biol. Chem. 289 (2014) 13661–13666. [DOI] [PMID: 24668807]
[EC 1.13.11.63 created 2012 (EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, incorporated 2015), modified 2016]
 
 
EC 1.13.11.71     
Accepted name: carotenoid-9′,10′-cleaving dioxygenase
Reaction: all-trans-β-carotene + O2 = all-trans-10′-apo-β-carotenal + β-ionone
For diagram of 10′-apo-β-carotenal biosynthesis, click here
Other name(s): BCO2 (gene name); β-carotene 9′,10′-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9′,10′-cleaving)
Systematic name: all-trans-β-carotene:oxygen oxidoreductase (9′,10′-cleaving)
Comments: Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E. and von Lintig, J. Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J. Biol. Chem. 276 (2001) 14110–14116. [DOI] [PMID: 11278918]
2.  Lindqvist, A., He, Y.G. and Andersson, S. Cell type-specific expression of β-carotene 9′,10′-monooxygenase in human tissues. J. Histochem. Cytochem. 53 (2005) 1403–1412. [DOI] [PMID: 15983114]
[EC 1.13.11.71 created 2012]
 
 
EC 1.13.12.7     
Accepted name: firefly luciferase
Reaction: D-firefly luciferin + O2 + ATP = firefly oxyluciferin + CO2 + AMP + diphosphate + hν
For diagram of reaction, click here
Glossary: D-firefly luciferin = Photinus-luciferin = (S)-4,5-dihydro-2-(6-hydroxy-1,3-benzothiazol-2-yl)thiazole-4-carboxylate
firefly oxyluciferin = 4,5-dihydro-2-(6-hydroxy-1,3-benzothiazol-2-yl)thiazol-4-one
Other name(s): Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Systematic name: D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Comments: The enzyme, which is found in fireflies (Lampyridae), is responsible for their biolouminescence. The reaction begins with the formation of an acid anhydride between the carboxylic group of D-firefly luciferin and AMP, with the release of diphosphate. An oxygenation follows, with release of the AMP group and formation of a very short-lived peroxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone (rather than the hydrolysis of the adenylate) releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of oxyluciferin. The excited luciferin then emits a photon, returning to its ground state. The enzyme has a secondary acyl-CoA ligase activity when acting on L-firefly luciferin (see EC 6.2.1.52).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61970-00-1
References:
1.  Green, A. A. and McElroy, W. D. Crystalline firefly luciferase. Biochim. Biophys. Acta 20 (1956) 170–176. [DOI] [PMID: 13315363]
2.  White, E.H., McCapra, F., Field, G.F. and McElroy, W.D. The structure and synthesis of firefly luciferin. J. Am. Chem. Soc. 83 (1961) 2402–2403.
3.  Hopkins, T.A., Seliger, H.H., White, E.H. and Cass, M.W. The chemiluminescence of firefly luciferin. A model for the bioluminescent reaction and identification of the product excited state. J. Am. Chem. Soc. 89 (1967) 7148–7150. [PMID: 6064360]
4.  White, E.H., Rapaport, E., Hopkins, T.A. and Seliger, H.H. Chemi- and bioluminescence of firefly luciferin. J. Am. Chem. Soc. 91 (1969) 2178–2180. [PMID: 5784183]
5.  Koo, J.A., Schmidt, S.P. and Schuster, G.B. Bioluminescence of the firefly: key steps in the formation of the electronically excited state for model systems. Proc. Natl. Acad. Sci. USA 75 (1978) 30–33. [DOI] [PMID: 272645]
6.  de Wet, J.R., Wood, K.V., Helinski, D.R. and DeLuca, M. Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proc. Natl. Acad. Sci. USA 82 (1985) 7870–7873. [DOI] [PMID: 3906652]
7.  Nakamura, M., Maki, S., Amano, Y., Ohkita, Y., Niwa, K., Hirano, T., Ohmiya, Y. and Niwa, H. Firefly luciferase exhibits bimodal action depending on the luciferin chirality. Biochem. Biophys. Res. Commun. 331 (2005) 471–475. [DOI] [PMID: 15850783]
8.  Sundlov, J.A., Fontaine, D.M., Southworth, T.L., Branchini, B.R. and Gulick, A.M. Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism. Biochemistry 51 (2012) 6493–6495. [DOI] [PMID: 22852753]
[EC 1.13.12.7 created 1976, modified 1981, modified 1982, modified 2017]
 
 
EC 1.13.99.1     
Accepted name: inositol oxygenase
Reaction: myo-inositol + O2 = D-glucuronate + H2O
For diagram of mammalian ascorbic-acid biosynthesis, click here
Other name(s): meso-inositol oxygenase; myo-inositol oxygenase; MOO
Systematic name: myo-inositol:oxygen oxidoreductase
Comments: An iron protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-59-8
References:
1.  Charalampous, F.C. Biochemical studies on inositol. V. Purification and properties of the enzyme that cleaves inositol to D-glucuronic acid. J. Biol. Chem. 234 (1959) 220–227. [PMID: 13630882]
2.  Reddy, C.C., Swan, J.S. and Hamilton, G.A. myo-Inositol oxygenase from hog kidney. I. Purification and characterization of the oxygenase and of an enzyme complex containing the oxygenase and D-glucuronate reductase. J. Biol. Chem. 256 (1981) 8510–8518. [PMID: 7263666]
3.  Arner, R.J., Prabhu, K.S., Thompson, J.T., Hildenbrandt, G.R., Liken, A.D. and Reddy, C.C. myo-Inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and D-chiro-inositol. Biochem. J. 360 (2001) 313–320. [PMID: 11716759]
[EC 1.13.99.1 created 1961 as EC 1.99.2.6, transferred 1965 to EC 1.13.1.11, transferred 1972 to EC 1.13.99.1, modified 2002]
 
 
EC 1.14.11.22      
Transferred entry: flavone synthase. Now EC 1.14.20.5, flavone synthase
[EC 1.14.11.22 created 2004, deleted 2018]
 
 
EC 1.14.11.48     
Accepted name: xanthine dioxygenase
Reaction: xanthine + 2-oxoglutarate + O2 = urate + succinate + CO2
For diagram of AMP catabolism, click here
Other name(s): XanA; α-ketoglutarate-dependent xanthine hydroxylase
Systematic name: xanthine,2-oxoglutarate:oxygen oxidoreductase
Comments: Requires Fe2+ and L-ascorbate. The enzyme, which was characterized from fungi, is specific for xanthine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cultrone, A., Scazzocchio, C., Rochet, M., Montero-Moran, G., Drevet, C. and Fernandez-Martin, R. Convergent evolution of hydroxylation mechanisms in the fungal kingdom: molybdenum cofactor-independent hydroxylation of xanthine via α-ketoglutarate-dependent dioxygenases. Mol. Microbiol. 57 (2005) 276–290. [DOI] [PMID: 15948966]
2.  Montero-Moran, G.M., Li, M., Rendon-Huerta, E., Jourdan, F., Lowe, D.J., Stumpff-Kane, A.W., Feig, M., Scazzocchio, C. and Hausinger, R.P. Purification and characterization of the FeII- and α-ketoglutarate-dependent xanthine hydroxylase from Aspergillus nidulans. Biochemistry 46 (2007) 5293–5304. [DOI] [PMID: 17429948]
3.  Li, M., Muller, T.A., Fraser, B.A. and Hausinger, R.P. Characterization of active site variants of xanthine hydroxylase from Aspergillus nidulans. Arch. Biochem. Biophys. 470 (2008) 44–53. [DOI] [PMID: 18036331]
[EC 1.14.11.48 created 2015]
 
 
EC 1.14.11.58     
Accepted name: ornithine lipid ester-linked acyl 2-hydroxylase
Reaction: an ornithine lipid + 2-oxoglutarate + O2 = a 2-hydroxyornithine lipid + succinate + CO2
Glossary: an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine
a 2-hydroxyornithine lipid = an Nα-[(3R)-3-(2-hydroxyacyloxy)acyl]-L-ornithine
Other name(s): olsC (gene name)
Systematic name: ornithine lipid,2-oxoglutarate:oxygen oxidoreductase (ester-linked acyl 2-hydroxylase)
Comments: The enzyme, characterized from the bacterium Rhizobium tropici, catalyses the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rojas-Jimenez, K., Sohlenkamp, C., Geiger, O., Martinez-Romero, E., Werner, D. and Vinuesa, P. A ClC chloride channel homolog and ornithine-containing membrane lipids of Rhizobium tropici CIAT899 are involved in symbiotic efficiency and acid tolerance. Mol. Plant Microbe Interact. 18 (2005) 1175–1185. [DOI] [PMID: 16353552]
2.  Vences-Guzman, M.A., Guan, Z., Ormeno-Orrillo, E., Gonzalez-Silva, N., Lopez-Lara, I.M., Martinez-Romero, E., Geiger, O. and Sohlenkamp, C. Hydroxylated ornithine lipids increase stress tolerance in Rhizobium tropici CIAT899. Mol. Microbiol. 79 (2011) 1496–1514. [DOI] [PMID: 21205018]
[EC 1.14.11.58 created 2018]
 
 
EC 1.14.13.8     
Accepted name: flavin-containing monooxygenase
Reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
Other name(s): dimethylaniline oxidase; dimethylaniline N-oxidase; FAD-containing monooxygenase; N,N-dimethylaniline monooxygenase; DMA oxidase; flavin mixed function oxidase; Ziegler’s enzyme; mixed-function amine oxidase; FMO; FMO-I; FMO-II; FMO1; FMO2; FMO3; FMO4; FMO5; flavin monooxygenase; methylphenyltetrahydropyridine N-monooxygenase; 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine:oxygen N-oxidoreductase; dimethylaniline monooxygenase (N-oxide-forming)
Systematic name: N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-73-8
References:
1.  Ziegler, D.M. and Pettit, F.H. Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes. Biochemistry 5 (1966) 2932–2938. [PMID: 4381353]
2.  Chiba, K., Kubota, E., Miyakawa, T., Kato, Y. and Ishizaki, T. Characterization of hepatic microsomal metabolism as an in vivo detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in mice. J. Pharmacol. Exp. Ther. 246 (1988) 1108–1115. [PMID: 3262153]
3.  Cashman, J.R. Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem. Res. Toxicol. 8 (1995) 165–181.
4.  Cashman, J.R. and Zhang, J. Human flavin-containing monooxygenases. Annu. Rev. Pharmacol. Toxicol. 46 (2006) 65–100. [DOI] [PMID: 16402899]
5.  Jones, K.C. and Ballou, D.P. Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J. Biol. Chem. 261 (1986) 2553–2559. [PMID: 3949735]
6.  Chiba, K., Kobayashi, K., Itoh, K., Itoh, S., Chiba, T., Ishizaki, T. and Kamataki, T. N-Oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the rat liver flavin-containing monooxygenase expressed in yeast cells. Eur. J. Pharmacol. 293 (1995) 97–100. [PMID: 7672012]
[EC 1.14.13.8 created 1972 (EC 1.13.12.11 created 1992, part-incorporated 2006), modified 2006]
 
 
EC 1.14.13.47      
Transferred entry: (S)-limonene 3-monooxygenase. Now EC 1.14.14.99, (S)-limonene 3-monooxygenase
[EC 1.14.13.47 created 1992, modified 2003, deleted 2018]
 
 
EC 1.14.13.48      
Transferred entry: (S)-limonene 6-monooxygenase. Now classified as EC 1.14.14.51, (S)-limonene 6-monooxygenase
[EC 1.14.13.48 created 1992, modified 2003, deleted 2017]
 
 
EC 1.14.13.49      
Transferred entry: (S)-limonene 7-monooxygenase. Now classified as EC 1.14.14.52, (S)-limonene 7-monooxygenase
[EC 1.14.13.49 created 1992, modified 2003, deleted 2017]
 
 
EC 1.14.13.59     
Accepted name: L-lysine N6-monooxygenase (NADPH)
Reaction: L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
For diagram of aerobactin biosynthesis, click here
Other name(s): lysine N6-hydroxylase; L-lysine 6-monooxygenase (NADPH) (ambiguous)
Systematic name: L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 64295-82-5
References:
1.  Plattner, H.J., Pfefferle, P., Romaguera, A., Waschutza, S. and Diekmann, H. Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222. Biol. Met. 2 (1989) 1–5. [PMID: 2518519]
2.  Macheroux, P., Plattner, H.J., Romaguera, A. and Diekmann, H. FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222. Eur. J. Biochem. 213 (1993) 995–1002. [DOI] [PMID: 8504838]
3.  Thariath, A.M., Fatum, K.L., Valvano, M.A. and Viswanatha, T. Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase. Biochim. Biophys. Acta 1203 (1993) 27–35. [DOI] [PMID: 8218389]
4.  de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523]
5.  Marrone, L., Siemann, S., Beecroft, M. and Viswanatha, T. Specificity of lysine:N-6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism. Bioorg. Chem. 24 (1996) 401–406.
6.  Goh, C.J., Szczepan, E.W., Menhart, N. and Viswanatha, T. Studies on lysine: N6-hydroxylation by cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 990 (1989) 240–245. [DOI] [PMID: 2493814]
[EC 1.14.13.59 created 1999, modified 2001, modified 2012]
 
 
EC 1.14.13.69     
Accepted name: alkene monooxygenase
Reaction: propene + NADH + H+ + O2 = 1,2-epoxypropane + NAD+ + H2O
For diagram of epoxide carboxylation, click here and for diagram of isoprene biosynthesis and metabolism, click here
Other name(s): alkene epoxygenase; etnABCD (gene names); amoABCDE (gene names)
Systematic name: alkene,NADH:oxygen oxidoreductase
Comments: This bacterial binuclear non-heme iron enzyme is a multicomponent enzyme complex comprising an oxygenase, a reductase, and a Rieske-type ferredoxin. The enzyme from the bacterium Xanthobacter sp. strain Py2 contains an additional small protein of unknown function that is essential for activity. In general, the enzyme oxygenates C2 to C6 aliphatic alkenes, although enzymes from different organisms show different substrate range. With propene as substrate, the stereospecificity of the epoxypropane formed is 95% (R) and 5% (S).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 63439-50-9
References:
1.  Small, F.J. and Ensign, S.A. Alkene monooxygenase from Xanthobacter strain Py2: purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes. J. Biol. Chem. 272 (1997) 24913–24920. [DOI] [PMID: 9312093]
2.  Gallagher, S.C., Cammack, R. and Dalton, H. Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions. Eur. J. Biochem. 247 (1997) 635–641. [DOI] [PMID: 9266707]
3.  Zhou, N.Y., Jenkins, A., Chion, C.K.N.C.K. and Leak, D.J. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Appl. Environ. Microbiol. 65 (1999) 1589–1595. [PMID: 10103255]
4.  Champreda, V., Zhou, N.Y. and Leak, D.J. Heterologous expression of alkene monooxygenase components from Xanthobacter autotrophicus Py2 and reconstitution of the active complex. FEMS Microbiol. Lett. 239 (2004) 309–318. [DOI] [PMID: 15476981]
5.  Champreda, V., Choi, Y.J., Zhou, N.Y. and Leak, D.J. Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions. Appl. Microbiol. Biotechnol. 71 (2006) 840–847. [DOI] [PMID: 16402171]
[EC 1.14.13.69 created 2001]
 
 
EC 1.14.13.88      
Transferred entry: flavanoid 3,5-hydroxylase. Now EC 1.14.14.81, flavanoid 3,5-hydroxylase
[EC 1.14.13.88 created 2004, deleted 2018]
 
 
EC 1.14.13.112      
Transferred entry: 3-epi-6-deoxocathasterone 23-monooxygenase. Now EC 1.14.14.147, 3-epi-6-deoxocathasterone 23-monooxygenase
[EC 1.14.13.112 created 2010, deleted 2018]
 
 
EC 1.14.13.156      
Transferred entry: 1,8-cineole 2-endo-monooxygenase. Now EC 1.14.14.133, 1,8-cineole 2-endo-monooxygenase
[EC 1.14.13.156 created 2012, deleted 2018]
 
 
EC 1.14.13.160     
Accepted name: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase
Reaction: [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + O2 + NADPH + H+ = [(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA + NADP+ + H2O
For diagram of camphor catabolism, click here
Glossary: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA = 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA
Other name(s): 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase; 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase; OTEMO
Systematic name: [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA,NADPH:oxygen oxidoreductase (1,5-lactonizing)
Comments: A FAD dependent enzyme isolated from Pseudomonas putida. Forms part of the catabolism pathway of camphor. It acts on the CoA ester in preference to the free acid.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ougham, H.J., Taylor, D.G. and Trudgill, P.W. Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida. J. Bacteriol. 153 (1983) 140–152. [PMID: 6848481]
2.  Leisch, H., Shi, R., Grosse, S., Morley, K., Bergeron, H., Cygler, M., Iwaki, H., Hasegawa, Y. and Lau, P.C. Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453. Appl. Environ. Microbiol. 78 (2012) 2200–2212. [DOI] [PMID: 22267661]
3.  Kadow, M., Loschinski, K., Sass, S., Schmidt, M. and Bornscheuer, U.T. Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization. Appl. Microbiol. Biotechnol. 96 (2012) 419–429. [DOI] [PMID: 22286514]
[EC 1.14.13.160 created 2012]
 
 
EC 1.14.13.161     
Accepted name: (+)-camphor 6-exo-hydroxylase
Reaction: (+)-camphor + NADPH + H+ + O2 = (+)-6-exo-hydroxycamphor + NADP+ + H2O
For diagram of camphor catabolism, click here
Other name(s): (+)-camphor 6-hydroxylase
Systematic name: (+)-camphor,NADPH:oxygen oxidoreductase (6-exo-hydroxylating)
Comments: A cytochrome P-450 monooxygenase isolated from Salvia officinalis (sage). Involved in the catabolism of camphor in senescent tissue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Funk, C., Koepp, A.E. and Croteau, R. Catabolism of camphor in tissue cultures and leaf disks of common sage (Salvia officinalis). Arch. Biochem. Biophys. 294 (1992) 306–313. [DOI] [PMID: 1550356]
2.  Funk, C. and Croteau, R. Induction and characterization of a cytochrome P-450-dependent camphor hydroxylase in tissue cultures of common sage (Salvia officinalis). Plant Physiol. 101 (1993) 1231–1237. [PMID: 12231778]
[EC 1.14.13.161 created 2012]
 
 
EC 1.14.13.162      
Transferred entry: 2,5-diketocamphane 1,2-monooxygenase. Now EC 1.14.14.108, 2,5-diketocamphane 1,2-monooxygenase
[EC 1.14.13.162 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, deleted 2018]
 
 
EC 1.14.13.190      
Transferred entry: ferruginol synthase. Now EC 1.14.14.175, ferruginol synthase
[EC 1.14.13.190 created 2014, modified 2015, deleted 2020]
 
 
EC 1.14.13.211     
Accepted name: rifampicin monooxygenase
Reaction: rifampicin + NAD(P)H + O2 = 2-hydroxy-2,27-secorifampicin + NAD(P)+ + H2O
For diagram of rifampicin, click here
Glossary: rifampicin = (2S,12Z,14E,16S,17S,18R,19R,20R,21S,22R,23S,24E)-5,6,9,17,19-pentahydroxy-23-methoxy-2,4,12,16,18,20,22-heptamethyl-8-{[(E)-(4-methylpiperazin-1-yl)imino]methyl}-1,11-dioxo-1,2-dihydro-2,7-(epoxypentadeca-1,11,13-trienoimino)nathpho[2,1-b]furan-21-yl acetate
Other name(s): RIF-O; ROX; RIFMO; rifampicin:NAD(P)H:oxygen oxidoreductase (2′-N-hydroxyrifampicin-forming) (incorrect)
Systematic name: rifampicin:NAD(P)H:oxygen oxidoreductase (2-hydroxy-2,27-secorifampicin-forming; ring-cleaving)
Comments: The enzyme has been found in a variety of environmental bacteria, notably Rhodococcus, Nocardia, and Streptomyces. It hydroxylates C-2 of rifampicin leading to its macro-ring cleaving.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Andersen, S.J., Quan, S., Gowan, B. and Dabbs, E.R. Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic. Antimicrob. Agents Chemother. 41 (1997) 218–221. [PMID: 8980786]
2.  Hoshino, Y., Fujii, S., Shinonaga, H., Arai, K., Saito, F., Fukai, T., Satoh, H., Miyazaki, Y. and Ishikawa, J. Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance. J. Antibiot. (Tokyo) 63 (2010) 23–28. [DOI] [PMID: 19942945]
3.  Koteva, K., Cox, G., Kelso, J.K., Surette, M.D., Zubyk, H.L., Ejim, L., Stogios, P., Savchenko, A., Sørensen, D. and Wright, G.D. Rox, a rifamycin resistance enzyme with an unprecedented mechanism of action. Cell Chem Biol 25 (2018) 403–412.e5. [DOI] [PMID: 29398560]
4.  Liu, L.K., Dai, Y., Abdelwahab, H., Sobrado, P. and Tanner, J.J. Structural evidence for rifampicin monooxygenase inactivating rifampicin by cleaving Its ansa-bridge. Biochemistry 57 (2018) 2065–2068. [DOI] [PMID: 29578336]
[EC 1.14.13.211 created 2016, modified 2022]
 
 
EC 1.14.13.225     
Accepted name: F-actin monooxygenase
Reaction: [F-actin]-L-methionine + NADPH + O2 + H+ = [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
Other name(s): MICAL (gene name)
Systematic name: [F-actin]-L-methionine,NADPH:O2 S-oxidoreductase
Comments: The enzyme, characterized from the fruit fly Drosophila melanogaster, is a multi-domain oxidoreductase that acts as an F-actin disassembly factor. The enzyme selectively reduces two L-Met residues of F-actin, causing fragmentation of the filaments and preventing repolymerization [1]. Free methionine is not a substrate [2]. The reaction is stereospecific and generates the (R)-sulfoxide [3]. In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1) [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hung, R.J., Yazdani, U., Yoon, J., Wu, H., Yang, T., Gupta, N., Huang, Z., van Berkel, W.J. and Terman, J.R. Mical links semaphorins to F-actin disassembly. Nature 463 (2010) 823–827. [DOI] [PMID: 20148037]
2.  Hung, R.J., Pak, C.W. and Terman, J.R. Direct redox regulation of F-actin assembly and disassembly by Mical. Science 334 (2011) 1710–1713. [DOI] [PMID: 22116028]
3.  Hung, R.J., Spaeth, C.S., Yesilyurt, H.G. and Terman, J.R. SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics. Nat. Cell Biol. 15 (2013) 1445–1454. [DOI] [PMID: 24212093]
4.  Zucchini, D., Caprini, G., Pasterkamp, R.J., Tedeschi, G. and Vanoni, M.A. Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1. Arch. Biochem. Biophys. 515 (2011) 1–13. [DOI] [PMID: 21864500]
5.  Vitali, T., Maffioli, E., Tedeschi, G. and Vanoni, M.A. Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains. Arch. Biochem. Biophys. 593 (2016) 24–37. [DOI] [PMID: 26845023]
[EC 1.14.13.225 created 2016]
 
 
EC 1.14.14.8     
Accepted name: anthranilate 3-monooxygenase (FAD)
Reaction: anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O
Glossary: anthranilate = 2-aminobenzoate
Other name(s): anthranilate 3-hydroxylase; anthranilate hydroxylase
Systematic name: anthranilate,FADH2:oxygen oxidoreductase (3-hydroxylating)
Comments: This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which ensures ample supply of FAD to the monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, X., Dong, Y., Li, X., Ren, Y., Li, Y., Wang, W., Wang, L. and Feng, L. Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2. Microbiology 156 (2010) 589–595. [DOI] [PMID: 19942660]
[EC 1.14.14.8 created 2010]
 
 
EC 1.14.14.33     
Accepted name: ethylenediaminetetraacetate monooxygenase
Reaction: ethylenediaminetetraacetate + 2 FMNH2 + 2 O2 = ethylenediamine-N,N′-diacetate + 2 glyoxylate + 2 FMN + 2 H2O (overall reaction)
(1a) ethylenediaminetetraacetate + FMNH2 + O2 = ethylenediaminetriacetate + glyoxylate + FMN + H2O
(1b) ethylenediaminetriacetate + FMNH2 + O2 = ethylenediamine-N,N′-diacetate + glyoxylate + FMN + H2O
Glossary: ethylenediaminetetraacetate = EDTA
Systematic name: ethylenediaminetetraacetate,FMNH2:O2 oxidoreductase (glyoxylate-forming)
Comments: The enzyme is part of a two component system that also includes EC 1.5.1.42, FMN reductase (NADH), which provides reduced flavin mononucleotide for this enzyme. It acts on EDTA only when it is complexed with divalent cations such as Mg2+, Zn2+, Mn2+, Co2+, or Cu2+. While the enzyme has a substrate overlap with EC 1.14.14.10, nitrilotriacetate monooxygenase, it has a much wider substrate range, which includes nitrilotriacetate (NTA) and diethylenetriaminepentaacetate (DTPA) in addition to EDTA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Witschel, M., Nagel, S. and Egli, T. Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103. J. Bacteriol. 179 (1997) 6937–6943. [DOI] [PMID: 9371437]
2.  Payne, J.W., Bolton, H., Jr., Campbell, J.A. and Xun, L. Purification and characterization of EDTA monooxygenase from the EDTA-degrading bacterium BNC1. J. Bacteriol. 180 (1998) 3823–3827. [PMID: 9683478]
3.  Bohuslavek, J., Payne, J.W., Liu, Y., Bolton, H., Jr. and Xun, L. Cloning, sequencing, and characterization of a gene cluster involved in EDTA degradation from the bacterium BNC1. Appl. Environ. Microbiol. 67 (2001) 688–695. [DOI] [PMID: 11157232]
[EC 1.14.14.33 created 2016]
 
 
EC 1.14.14.60     
Accepted name: ferruginol monooxygenase
Reaction: ferruginol + [reduced NADPH—hemoprotein reductase] + O2 = 11-hydroxyferruginol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of carnosic acid, salviol and suginol diterpenoids biosynthesis, click here
Glossary: ferruginol = abieta-8,11,13-trien-12-ol
Other name(s): CYP76AH24; CYP76AH3
Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (11-hydroxyferruginol-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage) and Salvia miltiorrhiza (danshen). 11-Hydroxyferruginol is a precursor of carnosic acid, a potent antioxidant.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl. Acad. Sci. USA 113 (2016) 3681–3686. [DOI] [PMID: 26976595]
2.  Scheler, U., Brandt, W., Porzel, A., Rothe, K., Manzano, D., Bozic, D., Papaefthimiou, D., Balcke, G.U., Henning, A., Lohse, S., Marillonnet, S., Kanellis, A.K., Ferrer, A. and Tissier, A. Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast. Nat. Commun. 7:12942 (2016). [DOI] [PMID: 27703160]
3.  Guo, J., Ma, X., Cai, Y., Ma, Y., Zhan, Z., Zhou, Y.J., Liu, W., Guan, M., Yang, J., Cui, G., Kang, L., Yang, L., Shen, Y., Tang, J., Lin, H., Ma, X., Jin, B., Liu, Z., Peters, R.J., Zhao, Z.K. and Huang, L. Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones. New Phytol. 210 (2016) 525–534. [DOI] [PMID: 26682704]
[EC 1.14.14.60 created 2018]
 
 
EC 1.14.14.61     
Accepted name: carnosic acid synthase
Reaction: 11-hydroxyferruginol + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = carnosic acid + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O
For diagram of carnosic acid, salviol and suginol diterpenoids biosynthesis, click here
Glossary: carnosic acid = 11,12-dihydroxyabieta-8,11,13-trien-20-oic acid
Other name(s): CYP76AK6; CYP76AK7; CYP76AK8
Systematic name: 11-hydroxyferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage), S. miltiorrhiza (red sage), S. fruticosa (Greek sage) and Rosmarinus officinalis (Rosemary).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl. Acad. Sci. USA 113 (2016) 3681–3686. [DOI] [PMID: 26976595]
2.  Scheler, U., Brandt, W., Porzel, A., Rothe, K., Manzano, D., Bozic, D., Papaefthimiou, D., Balcke, G.U., Henning, A., Lohse, S., Marillonnet, S., Kanellis, A.K., Ferrer, A. and Tissier, A. Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast. Nat. Commun. 7:12942 (2016). [DOI] [PMID: 27703160]
[EC 1.14.14.61 created 2018]
 
 
EC 1.14.14.62     
Accepted name: salviol synthase
Reaction: ferruginol + [reduced NADPH—hemoprotein reductase] + O2 = salviol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of carnosic acid, salviol and suginol diterpenoids biosynthesis, click here
Glossary: salviol = abieta-8,11,13-triene-2α,12-diol
Other name(s): CYP71BE52
Systematic name: ferruginol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (salviol-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Salvia pomifera (apple sage).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ignea, C., Athanasakoglou, A., Ioannou, E., Georgantea, P., Trikka, F.A., Loupassaki, S., Roussis, V., Makris, A.M. and Kampranis, S.C. Carnosic acid biosynthesis elucidated by a synthetic biology platform. Proc. Natl. Acad. Sci. USA 113 (2016) 3681–3686. [DOI] [PMID: 26976595]
[EC 1.14.14.62 created 2018]
 
 
EC 1.14.14.81     
Accepted name: flavanoid 3′,5′-hydroxylase
Reaction: a flavanone + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = a 3′,5′-dihydroxyflavanone + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 3′-hydroxyflavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′,5′-dihydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of myricetin biosynthesis, click here, for diagram of the biosynthesis of naringenin derivatives, click here and for diagram of flavonoid biosynthesis, click here
Other name(s): flavonoid 3′,5′-hydroxylase
Systematic name: flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′,5′-dihydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The 3′,5′-dihydroxyflavanone is formed via the 3′-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4′-trihydroxyflavanone (naringenin) at either the 3′ position to form eriodictyol or at both the 3′ and 5′ positions to form 5,7,3′,4′,5′-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3′,4′-pentahydroxyflavanone (taxifolin) at the 5′ position, forming ampelopsin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-23-1
References:
1.  Menting, J., Scopes, R.K. and Stevenson, T.W. Characterization of flavonoid 3′,5′-hydroxylase in microsomal membrane fraction of Petunia hybrida flowers. Plant Physiol. 106 (1994) 633–642. [PMID: 12232356]
2.  Shimada, Y., Nakano-Shimada, R., Ohbayashi, M., Okinaka, Y., Kiyokawa, S. and Kikuchi, Y. Expression of chimeric P450 genes encoding flavonoid-3′, 5′-hydroxylase in transgenic tobacco and petunia plants1. FEBS Lett. 461 (1999) 241–245. [DOI] [PMID: 10567704]
3.  de Vetten, N., ter Horst, J., van Schaik, H.P., de Boer, A., Mol, J. and Koes, R. A cytochrome b5 is required for full activity of flavonoid 3′, 5′-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors. Proc. Natl. Acad. Sci. USA 96 (1999) 778–783. [DOI] [PMID: 9892710]
[EC 1.14.14.81 created 2004 as EC 1.14.13.88, transferred 2018 to EC 1.14.14.81]
 
 
EC 1.14.14.108     
Accepted name: 2,5-diketocamphane 1,2-monooxygenase
Reaction: (+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
For diagram of camphor catabolism, click here
Glossary: (+)-bornane-2,5-dione = 2,5-diketocamphane
Other name(s): 2,5-diketocamphane lactonizing enzyme; ketolactonase I (ambiguous); 2,5-diketocamphane 1,2-monooxygenase oxygenating component; 2,5-DKCMO; camP (gene name); camphor 1,2-monooxygenase; camphor ketolactonase I
Systematic name: (+)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Comments: A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (+)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-3]. Can accept several bicyclic ketones including (+)- and (–)-camphor [6] and adamantanone [4]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc
References:
1.  Conrad, H.E., DuBus, R., Namtvedt, M.J. and Gunsalus, I.C. Mixed function oxidation. II. Separation and properties of the enzymes catalyzing camphor lactonizaton. J. Biol. Chem. 240 (1965) 495–503. [PMID: 14253460]
2.  Yu, C.A. and Gunsalus, I.C. Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components. J. Biol. Chem. 244 (1969) 6149–6152. [PMID: 4310834]
3.  Taylor, D.G. and Trudgill, P.W. Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453. J. Bacteriol. 165 (1986) 489–497. [DOI] [PMID: 3944058]
4.  Selifonov, S.A. Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid. Biochem. Biophys. Res. Commun. 186 (1992) 1429–1436. [DOI] [PMID: 1510672]
5.  Jones, K.H., Smith, R.T. and Trudgill, P.W. Diketocamphane enantiomer-specific ’Baeyer-Villiger’ monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J. Gen. Microbiol. 139 (1993) 797–805. [DOI] [PMID: 8515237]
6.  Kadow, M., Sass, S., Schmidt, M. and Bornscheuer, U.T. Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007. AMB Express 1:13 (2011). [DOI] [PMID: 21906366]
7.  Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. and Lau, P.C. Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79 (2013) 3282–3293. [PMID: 23524667]
[EC 1.14.14.108 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, transferred 2018 to EC 1.14.14.108]
 
 
EC 1.14.14.133     
Accepted name: 1,8-cineole 2-endo-monooxygenase
Reaction: 1,8-cineole + [reduced flavodoxin] + O2 = 2-endo-hydroxy-1,8-cineole + [oxidized flavodoxin] + H2O
For diagram of 1,8-cineole catabolism, click here
Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
2-endo-hydroxy-1,8-cineole = (1R,4S,6R)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-ol
Other name(s): P450cin; CYP176A; CYP176A1
Systematic name: 1,8-cineole,[reduced flavodoxin]:oxygen oxidoreductase (2-endo-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein that uses a flavodoxin-like redox partner to reduce the heme iron. Isolated from the bacterium Citrobacter braakii, which can use 1,8-cineole as the sole source of carbon.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. Cytochrome P450cin (CYP176A), isolation, expression, and characterization. J. Biol. Chem. 277 (2002) 27725–27732. [DOI] [PMID: 12016226]
2.  Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam. Biochemistry 43 (2004) 9487–9494. [DOI] [PMID: 15260491]
3.  Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin. J. Biol. Chem. 282 (2007) 27006–27011. [DOI] [PMID: 17606612]
4.  Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin. J. Biol. Chem. 283 (2008) 10804–10812. [DOI] [PMID: 18270198]
[EC 1.14.14.133 created 2012 as EC 1.14.13.156, transferred 2018 to EC 1.14.14.133]
 
 
EC 1.14.14.155     
Accepted name: 3,6-diketocamphane 1,2-monooxygenase
Reaction: (–)-bornane-2,5-dione + O2 + FMNH2 = (–)-5-oxo-1,2-campholide + FMN + H2O
Glossary: (–)-bornane-2,5-dione = 3,6-diketocamphane
Other name(s): 3,6-diketocamphane lactonizing enzyme; 3,6-DKCMO
Systematic name: (–)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Comments: A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (–)-camphor. Requires a dedicated NADH—FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1,2]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. and Lau, P.C. Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79 (2013) 3282–3293. [PMID: 23524667]
2.  Isupov, M.N., Schroder, E., Gibson, R.P., Beecher, J., Donadio, G., Saneei, V., Dcunha, S.A., McGhie, E.J., Sayer, C., Davenport, C.F., Lau, P.C., Hasegawa, Y., Iwaki, H., Kadow, M., Balke, K., Bornscheuer, U.T., Bourenkov, G. and Littlechild, J.A. The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 2344–2353. [PMID: 26527149]
[EC 1.14.14.155 created 2018]
 
 
EC 1.14.14.175     
Accepted name: ferruginol synthase
Reaction: abieta-8,11,13-triene + [reduced NADPH—hemoprotein reductase] + O2 = ferruginol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of abietane diterpenoids biosynthesis, click here
Glossary: ferruginol = abieta-8,11,13-trien-12-ol
Other name(s): miltiradiene oxidase (incorrect); CYP76AH1; miltiradiene,NADPH:oxygen oxidoreductase (ferruginol forming) (incorrect)
Systematic name: abieta-8,11,13-triene,[reduced NADPH—hemoprotein reductase]:oxygen 12-oxidoreductase (ferruginol-forming)
Comments: A cytochrome P-450 (heme thiolate) enzyme found in some members of the Lamiaceae (mint family). The enzyme from Rosmarinus officinalis (rosemary) is involved in biosynthesis of carnosic acid, while the enzyme from the Chinese medicinal herb Salvia miltiorrhiza is involved in the biosynthesis of the tanshinones, abietane-type norditerpenoid naphthoquinones that are the main lipophilic bioactive components found in the plant.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Guo, J., Zhou, Y.J., Hillwig, M.L., Shen, Y., Yang, L., Wang, Y., Zhang, X., Liu, W., Peters, R.J., Chen, X., Zhao, Z.K. and Huang, L. CYP76AH1 catalyzes turnover of miltiradiene in tanshinones biosynthesis and enables heterologous production of ferruginol in yeasts. Proc. Natl. Acad. Sci. USA 110 (2013) 12108–12113. [DOI] [PMID: 23812755]
2.  Zi, J. and Peters, R.J. Characterization of CYP76AH4 clarifies phenolic diterpenoid biosynthesis in the Lamiaceae. Org. Biomol. Chem. 11 (2013) 7650–7652. [DOI] [PMID: 24108414]
3.  Bozic, D., Papaefthimiou, D., Bruckner, K., de Vos, R.C., Tsoleridis, C.A., Katsarou, D., Papanikolaou, A., Pateraki, I., Chatzopoulou, F.M., Dimitriadou, E., Kostas, S., Manzano, D., Scheler, U., Ferrer, A., Tissier, A., Makris, A.M., Kampranis, S.C. and Kanellis, A.K. Towards elucidating carnosic acid biosynthesis in Lamiaceae: functional characterization of the three first steps of the pathway in Salvia fruticosa and Rosmarinus officinalis. PLoS One 10:e0124106 (2015). [DOI] [PMID: 26020634]
[EC 1.14.14.175 created 2014 as EC 1.14.13.190, modified 2015, transferred 2020 to EC 1.14.14.175]
 
 
EC 1.14.14.178     
Accepted name: steroid 22S-hydroxylase
Reaction: (1) a C27-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C27-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(2) a C28-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C28-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(3) a C29-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C29-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
Other name(s): CYP90B1 (gene name); DWF4 (gene name); steroid C-22 hydroxylase
Systematic name: steroid,NADPH—hemoprotein reductase:oxygen 22S-oxidoreductase (hydroxylating)
Comments: This plant cytochrome P-450 (heme thiolate) enzyme participates in the biosynthesis of brassinosteroids. While in vivo substrates include C28-steroids such as campestanol, campesterol, and 6-oxocampestanol, the enzyme is able to catalyse the C-22 hydroxylation of a variety of C27, C28 and C29 steroids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Asami, T., Mizutani, M., Fujioka, S., Goda, H., Min, Y.K., Shimada, Y., Nakano, T., Takatsuto, S., Matsuyama, T., Nagata, N., Sakata, K. and Yoshida, S. Selective interaction of triazole derivatives with DWF4, a cytochrome P450 monooxygenase of the brassinosteroid biosynthetic pathway, correlates with brassinosteroid deficiency in planta. J. Biol. Chem. 276 (2001) 25687–25691. [DOI] [PMID: 11319239]
2.  Choe, S., Fujioka, S., Noguchi, T., Takatsuto, S., Yoshida, S. and Feldmann, K.A. Overexpression of DWARF4 in the brassinosteroid biosynthetic pathway results in increased vegetative growth and seed yield in Arabidopsis. Plant J. 26 (2001) 573–582. [DOI] [PMID: 11489171]
3.  Asami, T., Mizutani, M., Shimada, Y., Goda, H., Kitahata, N., Sekimata, K., Han, S.Y., Fujioka, S., Takatsuto, S., Sakata, K. and Yoshida, S. Triadimefon, a fungicidal triazole-type P450 inhibitor, induces brassinosteroid deficiency-like phenotypes in plants and binds to DWF4 protein in the brassinosteroid biosynthesis pathway. Biochem. J. 369 (2003) 71–76. [DOI] [PMID: 12350224]
4.  Fujita, S., Ohnishi, T., Watanabe, B., Yokota, T., Takatsuto, S., Fujioka, S., Yoshida, S., Sakata, K. and Mizutani, M. Arabidopsis CYP90B1 catalyses the early C-22 hydroxylation of C27, C28 and C29 sterols. Plant J. 45 (2006) 765–774. [DOI] [PMID: 16460510]
5.  Ohnishi, T., Watanabe, B., Sakata, K. and Mizutani, M. CYP724B2 and CYP90B3 function in the early C-22 hydroxylation steps of brassinosteroid biosynthetic pathway in tomato. Biosci. Biotechnol. Biochem. 70 (2006) 2071–2080. [DOI] [PMID: 16960392]
[EC 1.14.14.178 created 2022]
 
 
EC 1.14.15.1     
Accepted name: camphor 5-monooxygenase
Reaction: (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
For diagram of camphor catabolism, click here
Other name(s): camphor 5-exo-methylene hydroxylase; 2-bornanone 5-exo-hydroxylase; bornanone 5-exo-hydroxylase; camphor 5-exo-hydroxylase; camphor 5-exohydroxylase; camphor hydroxylase; d-camphor monooxygenase; methylene hydroxylase; methylene monooxygenase; D-camphor-exo-hydroxylase; camphor methylene hydroxylase
Systematic name: (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating)
Comments: A heme-thiolate protein (P-450). Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-82-4
References:
1.  Hedegaard, J. and Gunsalus, I.C. Mixed function oxidation. IV. An induced methylene hydroxylase in camphor oxidation. J. Biol. Chem. 240 (1965) 4038–4043. [PMID: 4378858]
2.  Tyson, C.A., Lipscomb, J.D. and Gunsalus, I.C. The role of putidaredoxin and P450cam in methylene hydroxylation. J. Biol. Chem. 247 (1972) 5777–5784. [PMID: 4341491]
[EC 1.14.15.1 created 1972, modified 1986]
 
 
EC 1.14.15.2      
Transferred entry: camphor 1,2-monooxygenase. Now EC 1.14.13.162, 2,5-diketocamphane 1,2-monooxygenase.
[EC 1.14.15.2 created 1972, deleted 2012]
 
 
EC 1.14.15.8     
Accepted name: steroid 15β-monooxygenase
Reaction: progesterone + 2 reduced [2Fe-2S] ferredoxin + O2 = 15β-hydroxyprogesterone + 2 oxidized [2Fe-2S] ferredoxin + H2O
Other name(s): cytochrome P-450meg; cytochrome P450meg; steroid 15β-hydroxylase; CYP106A2; BmCYP106A2
Systematic name: progesterone,reduced-ferredoxin:oxygen oxidoreductase (15β-hydroxylating)
Comments: The enzyme from the bacterium Bacillus megaterium hydroxylates a variety of 3-oxo-Δ4-steroids in position 15β. Ring A-reduced, aromatic, and 3β-hydroxy-Δ4-steroids do not serve as substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264–5271. [PMID: 109432]
2.  Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J. Biol. Chem. 251 (1976) 2831–2838. [PMID: 177422]
3.  Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry. Biochem. Biophys. Res. Commun. 319 (2004) 677–682. [DOI] [PMID: 15178459]
4.  Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368. Biochim. Biophys. Acta 1794 (2009) 1635–1642. [DOI] [PMID: 19635596]
5.  Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. ChemBioChem 9 (2008) 1439–1449. [DOI] [PMID: 18481342]
[EC 1.14.15.8 created 2010]
 
 
EC 1.14.15.10     
Accepted name: (+)-camphor 6-endo-hydroxylase
Reaction: (+)-camphor + reduced putidaredoxin + O2 = (+)-6-endo-hydroxycamphor + oxidized putidaredoxin + H2O
For diagram of camphor catabolism, click here
Other name(s): P450camr
Systematic name: (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (6-endo-hydroxylating)
Comments: A cytochrome P-450 monooxygenase from the bacterium Rhodococcus sp. NCIMB 9784.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Grogan, G., Roberts, G.A., Parsons, S., Turner, N.J. and Flitsch, S.L. P450camr, a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor. Appl. Microbiol. Biotechnol. 59 (2002) 449–454. [DOI] [PMID: 12172608]
[EC 1.14.15.10 created 2012]
 
 
EC 1.14.19.4     
Accepted name: acyl-lipid (11-3)-desaturase
Reaction: (1) an (11Z,14Z)-icosa-11,14-dienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2) an (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Glossary: di-homo-γ-linolenate = (8Z,11Z,14Z)-icosa-8,11,14-trienoate
Other name(s): acyl-lipid 8-desaturase; Δ8 fatty acid desaturase; Δ8-desaturase; Δ8-fatty-acid desaturase; efd1 (gene name); D8Des (gene name); phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase (incorrect); SLD
Systematic name: acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase [(11-3),(11-2)-cis-dehydrogenating]
Comments: The enzyme, characterized from the protist Euglena gracilis [1] and the microalga Rebecca salina [2], introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Δ11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wallis, J.G. and Browse, J. The Δ8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids. Arch. Biochem. Biophys. 365 (1999) 307–316. [DOI] [PMID: 10328826]
2.  Zhou, X.R., Robert, S.S., Petrie, J.R., Frampton, D.M., Mansour, M.P., Blackburn, S.I., Nichols, P.D., Green, A.G. and Singh, S.P. Isolation and characterization of genes from the marine microalga Pavlova salina encoding three front-end desaturases involved in docosahexaenoic acid biosynthesis. Phytochemistry 68 (2007) 785–796. [DOI] [PMID: 17291553]
[EC 1.14.19.4 created 2008, modified 2015]
 
 
EC 1.14.19.5     
Accepted name: acyl-CoA 11-(Z)-desaturase
Reaction: an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Other name(s): Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase; acyl-CoA,hydrogen donor:oxygen Δ11-oxidoreductase; Δ11-fatty-acid desaturase
Systematic name: acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (11,12 cis-dehydrogenating)
Comments: The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs. In moths the enzyme participates in the biosynthesis of their sex pheromones. The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0) [4], that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0) [5], while that from the moth Spodoptera littoralis accepts both substrates [1]. The enzyme contains three histidine boxes that are conserved in all desaturases [2]. It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Martinez, T., Fabrias, G. and Camps, F. Sex pheromone biosynthetic pathway in Spodoptera littoralis and its activation by a neurohormone. J. Biol. Chem. 265 (1990) 1381–1387. [PMID: 2295634]
2.  Rodriguez, F., Hallahan, D.L., Pickett, J.A. and Camps, F. Characterization of the Δ11-palmitoyl-CoA-desaturase from Spodoptera littoralis (Lepidoptera:Noctuidae). Insect Biochem. Mol. Biol. 22 (1992) 143–148.
3.  Navarro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335–11336.
4.  Tonon, T., Harvey, D., Qing, R., Li, Y., Larson, T.R. and Graham, I.A. Identification of a fatty acid Δ11-desaturase from the microalga Thalassiosira pseudonana. FEBS Lett. 563 (2004) 28–34. [DOI] [PMID: 15063718]
5.  Hao, G., O'Connor, M., Liu, W. and Roelofs, W.L. Characterization of Z/E11- and Z9-desaturases from the obliquebanded leafroller moth, Choristoneura rosaceana. J. Insect Sci. 2:26 (2002) 1–7. [PMID: 15455060]
[EC 1.14.19.5 created 2008 (EC 1.14.99.32 created 2000, incorporated 2015), modified 2015]
 
 


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