The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 1.14.99.3      
Transferred entry: heme oxygenase (biliverdin-producing). Now EC 1.14.14.18, heme oxygenase (biliverdin-producing)
[EC 1.14.99.3 created 1972, modified 2006, deleted 2015]
 
 
EC 1.14.99.30      
Transferred entry: carotene 7,8-desaturase. Now EC 1.3.5.6, 9,9′-dicis-ζ-carotene desaturase.
[EC 1.14.99.30 created 1999, deleted 2011]
 
 
EC 1.14.99.31      
Transferred entry: myristoyl-CoA 11-(E) desaturase. Now classified as EC 1.14.19.24, myristoyl-CoA 11-(E) desaturase
[EC 1.14.99.31 created 2000, deleted 2015]
 
 
EC 1.14.99.32      
Transferred entry: myristoyl-CoA 11-(Z) desaturase. Now classified as EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase.
[EC 1.14.99.32 created 2000, deleted 2015]
 
 
EC 1.14.99.33      
Transferred entry: Δ12-fatty acid dehydrogenase. Now EC 1.14.19.39, acyl-lipid Δ12-acetylenase
[EC 1.14.99.33 created 2000, deleted 2015]
 
 
EC 1.14.99.34     
Accepted name: monoprenyl isoflavone epoxidase
Reaction: 7-O-methylluteone + NADPH + H+ + O2 = dihydrofurano derivatives + NADP+ + H2O
Glossary: luteone = 3-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-(3-methyl-2-butenyl)-4H-1-benzopyran-4-one
naringenin = 4′,5,7-trihydroxyflavan-4-one
Other name(s): monoprenyl isoflavone monooxygenase; 7-O-methylluteone:O2 oxidoreductase; 7-O-methylluteone,NADPH:O2 oxidoreductase
Systematic name: 7-O-methylluteone,NADPH:oxygen oxidoreductase
Comments: A flavoprotein (FAD) with high specificity for monoprenyl isoflavone. The product of the prenyl epoxidation reaction contains an oxygen atom derived from O2, but not from H2O. It is slowly and non-enzymically converted into the corresponding dihydrofurano derivative. The enzyme in the fungus Botrytis cinerea is induced by the substrate analogue, 6-prenylnaringenin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 198496-86-5
References:
1.  Tanaka, M. and Tahara, S. FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids. Phytochemistry 46 (1997) 433–439.
[EC 1.14.99.34 created 2000]
 
 
EC 1.14.99.35     
Accepted name: thiophene-2-carbonyl-CoA monooxygenase
Reaction: thiophene-2-carbonyl-CoA + reduced acceptor + O2 = 5-hydroxythiophene-2-carbonyl-CoA + acceptor + H2O
Other name(s): thiophene-2-carboxyl-CoA dehydrogenase; thiophene-2-carboxyl-CoA hydroxylase; thiophene-2-carboxyl-CoA monooxygenase
Systematic name: thiophene-2-carbonyl-CoA, hydrogen-donor:oxygen oxidoreductase
Comments: A molybdenum enzyme. Highly specific for thiophene-2-carbonyl-CoA. Tetrazolium salts can act as electron acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 208540-44-7
References:
1.  Bambauer, A., Rainey, F.A., Stackebrandt, E. and Winter, J. Characterization of Aquamicrobium defluvii gen. nov. sp. nov., a thiophene-2-carboxylate-metabolizing bacterium from activated sludge. Arch. Microbiol. 169 (1998) 293–302. [PMID: 9531630]
[EC 1.14.99.35 created 2000]
 
 
EC 1.14.99.36      
Transferred entry: β-carotene 15,15-monooxygenase. Now classified as EC 1.13.11.63, β-carotene 15,15′-dioxygenase.
[EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, deleted 2015]
 
 
EC 1.14.99.37     
Accepted name: taxadiene 5α-hydroxylase
Reaction: taxa-4,11-diene + reduced acceptor + O2 = taxa-4(20),11-dien-5α-ol + acceptor + H2O
For diagram of taxadiene hydroxylation, click here
Systematic name: taxa-4,11-diene,hydrogen-donor:oxygen oxidoreductase (5α-hydroxylating)
Comments: This microsomal cytochrome-P-450-dependent enzyme is involved in the biosynthesis of the diterpenoid antineoplastic drug Taxol (paclitaxel). The reaction includes rearrangement of the 4(5)-double bond to a 4(20)-double bond, possibly through allylic oxidation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9035-51-2
References:
1.  Hefner, J., Rubenstein, S.M., Ketchum, R.E., Gibson, D.M., Williams, R.M. and Croteau, R. Cytochrome P450-catalyzed hydroxylation of taxa-4(5),11(12)-diene to taxa-4(20),11(12)-dien-5α-ol: the first oxygenation step in taxol biosynthesis. Chem. Biol. 3 (1996) 479–489. [DOI] [PMID: 8807878]
[EC 1.14.99.37 created 2002]
 
 
EC 1.14.99.38     
Accepted name: cholesterol 25-hydroxylase
Reaction: cholesterol + reduced acceptor + O2 = 25-hydroxycholesterol + acceptor + H2O
For diagram of cholic acid biosynthesis (sidechain), click here
Glossary: cholesterol = cholest-5-en-3β-ol
Other name(s): cholesterol 25-monooxygenase
Systematic name: cholesterol,hydrogen-donor:oxygen oxidoreductase (25-hydroxylating)
Comments: Unlike most other sterol hydroxylases, this enzyme is not a cytochrome P-450. Instead, it uses diiron cofactors to catalyse the hydroxylation of hydrophobic substrates [1]. The diiron cofactor can be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through interactions with clustered histidine or glutamate residues [4,5]. In cell cultures, this enzyme down-regulates cholesterol synthesis and the processing of sterol regulatory element binding proteins (SREBPs).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-07-5
References:
1.  Lund, E.G., Kerr, T.A., Sakai, J., Li, W.P. and Russell, D.W. cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism. J. Biol. Chem. 273 (1998) 34316–34327. [DOI] [PMID: 9852097]
2.  Chen, J.J., Lukyanenko, Y. and Hutson, J.C. 25-Hydroxycholesterol is produced by testicular macrophages during the early postnatal period and influences differentiation of Leydig cells in vitro. Biol. Reprod. 66 (2002) 1336–1341. [PMID: 11967195]
3.  Lukyanenko, Y., Chen, J.J. and Hutson, J.C. Testosterone regulates 25-hydroxycholesterol production in testicular macrophages. Biol. Reprod. 67 (2002) 1435–1438. [PMID: 12390873]
4.  Fox, B.G., Shanklin, J., Ai, J., Loehr, T.M. and Sanders-Loehr, J. Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins. Biochemistry 33 (1994) 12776–12786. [PMID: 7947683]
5.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
[EC 1.14.99.38 created 2005]
 
 
EC 1.14.99.39     
Accepted name: ammonia monooxygenase
Reaction: NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O
Other name(s): AMO
Systematic name: ammonia,donor:oxygen oxidoreductase (hydroxylamine-producing)
Comments: The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper [1], iron [5] and possibly zinc [9]. The enzyme requires two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Ensign, S.A., Hyman, M.R. and Arp, D.J. In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper. J. Bacteriol. 175 (1993) 1971–1980. [DOI] [PMID: 8458839]
2.  Hyman, M.R., Page, C.L. and Arp, D.J. Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea. Appl. Environ. Microbiol. 60 (1994) 3033–3035. [PMID: 8085841]
3.  Bergmann, D.J. and Hooper, A.B. Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea. Biochem. Biophys. Res. Commun. 204 (1994) 759–762. [DOI] [PMID: 7980540]
4.  Holmes, A.J., Costello, A., Lidstrom, M.E. and Murrell, J.C. Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related. FEMS Microbiol. Lett. 132 (1995) 203–208. [DOI] [PMID: 7590173]
5.  Zahn, J.A., Arciero, D.M., Hooper, A.B. and DiSpirito, A.A. Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea. FEBS Lett. 397 (1996) 35–38. [DOI] [PMID: 8941709]
6.  Moir, J.W., Crossman, L.C., Spiro, S. and Richardson, D.J. The purification of ammonia monooxygenase from Paracoccus denitrificans. FEBS Lett. 387 (1996) 71–74. [DOI] [PMID: 8654570]
7.  Whittaker, M., Bergmann, D., Arciero, D. and Hooper, A.B. Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea. Biochim. Biophys. Acta 1459 (2000) 346–355. [DOI] [PMID: 11004450]
8.  Arp, D.J., Sayavedra-Soto, L.A. and Hommes, N.G. Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea. Arch. Microbiol. 178 (2002) 250–255. [DOI] [PMID: 12209257]
9.  Gilch, S., Meyer, O. and Schmidt, I. A soluble form of ammonia monooxygenase in Nitrosomonas europaea. Biol. Chem. 390 (2009) 863–873. [DOI] [PMID: 19453274]
[EC 1.14.99.39 created 2010]
 
 


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