The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: homomethionine N-monooxygenase
Reaction: an L-polyhomomethionine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = an (E)-ω-(methylsulfanyl)alkanal oxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) an L-polyhomomethionine + [reduced NADPH—hemoprotein reductase] + O2 = an L-N-hydroxypolyhomomethionine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) an L-N-hydroxypolyhomomethionine + [reduced NADPH—hemoprotein reductase] + O2 = an L-N,N-dihydroxypolyhomomethionine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) an L-N,N-dihydroxypolyhomomethionine = an (E)-ω-(methylsulfanyl)alkanal oxime + CO2 + H2O
Glossary: homomethionine = (2S)-2-amino-5-(methylsulfanyl)pentanoate
an L-polyhomomethionine = analogs of L-methionine that contain additional methylene groups in the side chain prior to the sulfur atom.
Other name(s): CYP79F1 (gene name); CYP79F2 (gene name)
Systematic name: L-polyhomomethionine,[NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This plant cytochrome P-450 (heme thiolate) enzyme is involved in methionine-derived aliphatic glucosinolates biosynthesis. It catalyses two successive N-hydroxylations, which are followed by dehydration and decarboxylation. CYP79F1 from Arabidopsis thaliana can metabolize mono-, di-, tri-, tetra-, penta-, and hexahomomethionine to their corresponding aldoximes, while CYP79F2 from the same plant can only metabolize penta- and hexahomomethionine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Hansen, C.H., Wittstock, U., Olsen, C.E., Hick, A.J., Pickett, J.A. and Halkier, B.A. Cytochrome p450 CYP79F1 from arabidopsis catalyzes the conversion of dihomomethionine and trihomomethionine to the corresponding aldoximes in the biosynthesis of aliphatic glucosinolates. J. Biol. Chem. 276 (2001) 11078–11085. [PMID: 11133994]
2.  Chen, S., Glawischnig, E., Jørgensen, K., Naur, P., Jorgensen, B., Olsen, C.E., Hansen, C.H., Rasmussen, H., Pickett, J.A. and Halkier, B.A. CYP79F1 and CYP79F2 have distinct functions in the biosynthesis of aliphatic glucosinolates in Arabidopsis. Plant J. 33 (2003) 923–937. [PMID: 12609033]
[EC created 2017]

Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald