The Enzyme Database

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EC 1.14.14.3     
Accepted name: bacterial luciferase
Reaction: a long-chain aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + H2O +
Other name(s): aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal monooxygenase (FMN); aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Systematic name: long-chain-aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Comments: The reaction sequence starts with the incorporation of a molecule of oxygen into reduced FMN bound to the enzyme, forming luciferase peroxyflavin. The peroxyflavin interacts with an aliphatic long-chain aldehyde, producing a highly fluorescent species believed to be luciferase hydroxyflavin. The enzyme is highly specific for reduced FMN and for long-chain aliphatic aldehydes with eight carbons or more. The highest efficiency is achieved with tetradecanal. cf. EC 1.13.12.18, dinoflagellate luciferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-00-0
References:
1.  Hastings, J.W. and Nealson, K.H. Bacterial bioluminescence. Annu. Rev. Microbiol. 31 (1977) 549–595. [DOI] [PMID: 199107]
2.  Hastings, J.W. Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde. Crit. Rev. Biochem. 5 (1978) 163–184. [PMID: 363350]
3.  Hastings, J.W. and Presswood, R.P. Bacterial luciferase: FMNH2-aldehyde oxidase. Methods Enzymol. 53 (1978) 558–570. [PMID: 309549]
4.  Nealson, K.H. and Hastings, J.W. Bacterial bioluminescence: its control and ecological significance. Microbiol. Rev. 43 (1979) 496–518. [PMID: 396467]
5.  Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T. O2 incorporation into a long-chain fatty-acid during bacterial luminescence. Biochim. Biophys. Acta 722 (1983) 297–301.
6.  Kurfurst, M., Ghisla, S. and Hastings, J.W. Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction. Proc. Natl. Acad. Sci. USA 81 (1984) 2990–2994. [DOI] [PMID: 16593462]
[EC 1.14.14.3 created 1981, modified 2016]
 
 
EC 1.14.14.30     
Accepted name: isobutylamine N-monooxygenase
Reaction: (1) 2-methylpropan-1-amine + FADH2 + O2 = N-(2-methylpropyl)hydroxylamine + FAD + H2O
(2) 2-methylpropan-1-amine + FMNH2 + O2 = N-(2-methylpropyl)hydroxylamine + FMN + H2O
Glossary: 2-methylpropan-1-amine = isobutylamine
N-(2-methylpropyl)hydroxylamine = N-hydroxy-2-methylpropan-1-amine = isobutylhydroxylamine
Other name(s): vlmH (gene name)
Systematic name: 2-methylpropan-1-amine,FADH2:O2 N-oxidoreductase
Comments: The enzyme, characterized from the bacterium Streptomyces viridifaciens, is part of a two component system that also includes a flavin reductase, which provides reduced flavin mononucleotide for this enzyme. The enzyme, which is involved in the biosynthesis of the azoxy antibiotic valanimycin, has a similar activity with either FMNH2 or FADH2. It exhibits broad specificity, and also accepts propan-1-amine, butan-1-amine, butan-2-amine and benzylamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Parry, R.J. and Li, W. Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens MG456-hF10. Arch. Biochem. Biophys. 339 (1997) 47–54. [DOI] [PMID: 9056232]
2.  Parry, R.J., Li, W. and Cooper, H.N. Cloning, analysis, and overexpression of the gene encoding isobutylamine N-hydroxylase from the valanimycin producer, Streptomyces viridifaciens. J. Bacteriol. 179 (1997) 409–416. [DOI] [PMID: 8990292]
3.  Parry, R.J. and Li, W. An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces viridifaciens. Cloning, analysis, and overexpression. J. Biol. Chem. 272 (1997) 23303–23311. [DOI] [PMID: 9287340]
[EC 1.14.14.30 created 2016, modified 2017]
 
 
EC 1.14.14.31     
Accepted name: ipsdienol synthase
Reaction: myrcene + [reduced NADPH—hemoprotein reductase] + O2 = (R)-ipsdienol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: myrcene = 7-methyl-3-methyleneocta-1,6-diene
ipsdienol = 2-methyl-6-methyleneocta-2,7-dien-4-ol
Other name(s): myrcene hydroxylase; CYP9T2; CYP9T3
Systematic name: myrcene,NADPH—hemoprotein reductase:O2 oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 heme-thiolate protein. Involved in the insect aggregation pheromone production. Isolated from the pine engraver beetle, Ips pini. A small amount of (S)-ipsdienol is also formed. In vitro it also hydroxylated (+)- and (–)-α-pinene, 3-carene, and (+)-limonene, but not α-phellandrene, (–)-β-pinene, γ-terpinene, or terpinolene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sandstrom, P., Welch, W.H., Blomquist, G.J. and Tittiger, C. Functional expression of a bark beetle cytochrome P450 that hydroxylates myrcene to ipsdienol. Insect Biochem. Mol. Biol. 36 (2006) 835–845. [DOI] [PMID: 17046597]
2.  Song, M., Kim, A.C., Gorzalski, A.J., MacLean, M., Young, S., Ginzel, M.D., Blomquist, G.J. and Tittiger, C. Functional characterization of myrcene hydroxylases from two geographically distinct Ips pini populations. Insect Biochem. Mol. Biol. 43 (2013) 336–343. [DOI] [PMID: 23376633]
[EC 1.14.14.31 created 2015 as EC 1.14.13.207, transferred 2016 to EC 1.14.14.31]
 
 
EC 1.14.14.32     
Accepted name: 17α-hydroxyprogesterone deacetylase
Reaction: (1) 17α-hydroxyprogesterone + [reduced NADPH—hemoprotein reductase] + O2 = androstenedione + acetate + [oxidized NADPH—hemoprotein reductase] + H2O
(2) 17α-hydroxypregnenolone + [reduced NADPH—hemoprotein reductase] + O2 = 3β-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: androstenedione = androst-4-ene-3,17-dione
Other name(s): C-17/C-20 lyase; 17α-hydroxyprogesterone acetaldehyde-lyase; CYP17; CYP17A1 (gene name); 17α-hydroxyprogesterone 17,20-lyase
Systematic name: 17α-hydroxyprogesterone,NADPH—hemoprotein reductase:oxygen oxidoreductase (17α-hydroxylating, acetate-releasing)
Comments: A microsomal cytochrome P-450 (heme-thiolate) protein that catalyses two independent reactions at the same active site - the 17-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis (EC 1.14.14.19), and the conversion of the 17-hydroxylated products via a 17,20-lyase reaction to form androstenedione and 3β-hydroxyandrost-5-en-17-one, leading to sex hormone biosynthesis. The activity of this reaction is dependent on the allosteric interaction of the enzyme with cytochrome b5 without any transfer of electrons from the cytochrome [2,4]. The enzymes from different organisms differ in their substrate specificity. While the enzymes from pig, hamster, and rat accept both 17α-hydroxyprogesterone and 17α-hydroxypregnenolone, the enzymes from human, bovine, sheep, goat, and bison do not accept the former, and the enzyme from guinea pig does not accept the latter [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-24-5
References:
1.  Gilep, A.A., Estabrook, R.W. and Usanov, S.A. Molecular cloning and heterologous expression in E. coli of cytochrome P45017α. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species. Biochemistry (Mosc.) 68 (2003) 86–98. [PMID: 12693981]
2.  Auchus, R.J., Lee, T.C. and Miller, W.L. Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273 (1998) 3158–3165. [DOI] [PMID: 9452426]
3.  Mak, P.J., Gregory, M.C., Denisov, I.G., Sligar, S.G. and Kincaid, J.R. Unveiling the crucial intermediates in androgen production. Proc. Natl. Acad. Sci. USA 112 (2015) 15856–15861. [DOI] [PMID: 26668369]
4.  Simonov, A.N., Holien, J.K., Yeung, J.C., Nguyen, A.D., Corbin, C.J., Zheng, J., Kuznetsov, V.L., Auchus, R.J., Conley, A.J., Bond, A.M., Parker, M.W., Rodgers, R.J. and Martin, L.L. Mechanistic scrutiny identifies a kinetic role for cytochrome b5 regulation of human cytochrome P450c17 (CYP17A1, P450 17A1). PLoS One 10:e0141252 (2015). [DOI] [PMID: 26587646]
5.  Bhatt, M.R., Khatri, Y., Rodgers, R.J. and Martin, L.L. Role of cytochrome b5 in the modulation of the enzymatic activities of cytochrome P450 17α-hydroxylase/17,20-lyase (P450 17A1). J. Steroid Biochem. Mol. Biol. (2016) . [DOI] [PMID: 26976652]
[EC 1.14.14.32 created 1976 as EC 4.1.2.30, transferred 2016 to EC 1.14.14.32]
 
 
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 1.14.14.34     
Accepted name: methanesulfonate monooxygenase (FMNH2)
Reaction: methanesulfonate + FMNH2 + O2 = formaldehyde + FMN + sulfite + H2O
Glossary: methanesulfonate = CH3-SO3-
formaldehyde = H-CHO
Other name(s): msuD (gene name); ssuD (gene name)
Systematic name: methanesulfonate,FMNH2:oxygen oxidoreductase
Comments: The enzyme, characterized from Pseudomonas strains, allows the organisms to utilize methanesulfonate as their sulfur source. It acts in combination with a dedicated NADH-dependent FMN reductase (EC 1.5.1.42), which provides it with reduced FMN. cf. EC 1.14.13.111, methanesulfonate monooxygenase (NADH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
References:
1.  Kertesz, M.A., Schmidt-Larbig, K. and Wuest, T. A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa. J. Bacteriol. 181 (1999) 1464–1473. [PMID: 10049377]
2.  Endoh, T., Kasuga, K., Horinouchi, M., Yoshida, T., Habe, H., Nojiri, H. and Omori, T. Characterization and identification of genes essential for dimethyl sulfide utilization in Pseudomonas putida strain DS1. Appl. Microbiol. Biotechnol. 62 (2003) 83–91. [DOI] [PMID: 12835925]
[EC 1.14.14.34 created 2016]
 
 
EC 1.14.14.35     
Accepted name: dimethylsulfone monooxygenase
Reaction: dimethyl sulfone + FMNH2 + O2 = methanesulfinate + formaldehyde + FMN + H2O
Other name(s): sfnG (gene name)
Systematic name: dimethyl sulfone,FMNH2:oxygen oxidoreductase
Comments: The enzyme, characterized from Pseudomonas spp., is involved in a dimethyl sulfide degradation pathway. It is dependent on NAD(P)H-dependent FMN reductase (EC 1.5.1.38, EC 1.5.1.39, or EC 1.5.1.42), which provides it with reduced FMN. The product, methanesulfinate, is oxidized spontaneously to methanesulfonate in the presence of dioxygen and FMNH2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Endoh, T., Habe, H., Nojiri, H., Yamane, H. and Omori, T. The σ54-dependent transcriptional activator SfnR regulates the expression of the Pseudomonas putida sfnFG operon responsible for dimethyl sulphone utilization. Mol. Microbiol. 55 (2005) 897–911. [DOI] [PMID: 15661012]
2.  Wicht, D.K. The reduced flavin-dependent monooxygenase SfnG converts dimethylsulfone to methanesulfinate. Arch. Biochem. Biophys. 604 (2016) 159–166. [DOI] [PMID: 27392454]
[EC 1.14.14.35 created 2016]
 
 
EC 1.14.14.36     
Accepted name: tyrosine N-monooxygenase
Reaction: L-tyrosine + 2 O2 + 2 [reduced NADPH—hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-tyrosine + O2 + [reduced NADPH—hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-tyrosine + O2 + [reduced NADPH—hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
For diagram of dhurrin biosynthesis, click here
Other name(s): tyrosine N-hydroxylase; CYP79A1
Systematic name: L-tyrosine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin. In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 159447-19-5
References:
1.  Halkier, B.A. and Møller, B.L. The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate. J. Biol. Chem. 265 (1990) 21114–21121. [PMID: 2250015]
2.  Sibbesen, O., Koch, B., Halkier, B.A. and Møller, B.L. Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 270 (1995) 3506–3511. [DOI] [PMID: 7876084]
3.  Bennett, R.N., Kiddle, G. and Wallsgrove, R.M. Involvement of cytochrome P450 in glucosinolate biosynthesis in white mustard (a biochemical anomaly). Plant Physiol. 114 (1997) 1283–1291. [PMID: 12223771]
4.  Kahn, R.A., Fahrendorf, T., Halkier, B.A. and Møller, B.L. Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 363 (1999) 9–18. [DOI] [PMID: 10049494]
5.  Bak, S., Olsen, C.E., Halkier, B.A. and Møller, B.L. Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in Dhurrin biosynthesis. Plant Physiol. 123 (2000) 1437–1448. [PMID: 10938360]
6.  Nielsen, J.S. and Møller, B.L. Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima. Plant Physiol. 122 (2000) 1311–1321. [PMID: 10759528]
7.  Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222–1231. [DOI] [PMID: 12114576]
8.  Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779–1784. [DOI] [PMID: 15665094]
9.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [DOI] [PMID: 26361733]
[EC 1.14.14.36 created 1992 as EC 1.14.13.41, modified 2001, modified 2005, transferred 2016 to EC 1.14.14.36]
 
 
EC 1.14.14.37     
Accepted name: 4-hydroxyphenylacetaldehyde oxime monooxygenase
Reaction: (E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) (E)-4-hydroxyphenylacetaldehyde oxime = (Z)-4-hydroxyphenylacetaldehyde oxime
(1b) (Z)-4-hydroxyphenylacetaldehyde oxime = 4-hydroxyphenylacetonitrile + H2O
(1c) 4-hydroxyphenylacetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of dhurrin biosynthesis, click here
Glossary: (S)-4-hydroxymandelonitrile = (2S)-hydroxy(4-hydroxyphenyl)acetonitrile
Other name(s): 4-hydroxybenzeneacetaldehyde oxime monooxygenase; cytochrome P450II-dependent monooxygenase; NADPH-cytochrome P450 reductase (CYP71E1); CYP71E1; 4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase
Systematic name: (E)-4-hydroxyphenylacetaldehyde oxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum. It catalyses three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  MacFarlane, I.J., Lees, E.M. and Conn, E.E. The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor. J. Biol. Chem. 250 (1975) 4708–4713. [PMID: 237909]
2.  Shimada, M. and Conn, E.E. The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile. Arch. Biochem. Biophys. 180 (1977) 199–207. [DOI] [PMID: 193443]
3.  Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222–1231. [DOI] [PMID: 12114576]
4.  Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779–1784. [DOI] [PMID: 15665094]
5.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [DOI] [PMID: 26361733]
[EC 1.14.14.37 created 2000 as EC 1.14.13.68, modified 2005, transferred 2016 to EC 1.14.14.37]
 
 
EC 1.14.14.38     
Accepted name: valine N-monooxygenase
Reaction: L-valine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-2-methylpropanal oxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-valine + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-valine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-valine + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-valine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-valine = (E)-2-methylpropanal oxime + CO2 + H2O
Other name(s): CYP79D1; CYP79D2
Systematic name: L-valine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Andersen, M.D., Busk, P.K., Svendsen, I. and Møller, B.L. Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes. J. Biol. Chem. 275 (2000) 1966–1975. [DOI] [PMID: 10636899]
2.  Forslund, K., Morant, M., Jørgensen, B., Olsen, C.E., Asamizu, E., Sato, S., Tabata, S. and Bak, S. Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus. Plant Physiol. 135 (2004) 71–84. [DOI] [PMID: 15122013]
[EC 1.14.14.38 created 2010 as EC 1.14.13.118, transferred 2017 to EC 1.14.14.38]
 
 
EC 1.14.14.39     
Accepted name: isoleucine N-monooxygenase
Reaction: L-isoleucine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-isoleucine + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-isoleucine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-isoleucine + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-isoleucine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-isoleucine = (1E,2S)-2-methylbutanal oxime + CO2 + H2O (spontaneous)
Other name(s): CYP79D3 (gene name); CYP79D4 (gene name)
Systematic name: L-isoleucine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-valine, but with a lower activity. cf. EC 1.14.14.38, valine N-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Andersen, M.D., Busk, P.K., Svendsen, I. and Møller, B.L. Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes. J. Biol. Chem. 275 (2000) 1966–1975. [DOI] [PMID: 10636899]
2.  Forslund, K., Morant, M., Jørgensen, B., Olsen, C.E., Asamizu, E., Sato, S., Tabata, S. and Bak, S. Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus. Plant Physiol. 135 (2004) 71–84. [DOI] [PMID: 15122013]
[EC 1.14.14.39 created 2010 as EC 1.14.13.117, transferred 2017 to EC 1.14.14.39]
 
 


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