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EC 1.14.19.52 Details
show Brenda entryEC number
1.14.19.52
Accepted name
camalexin synthase
Reaction
2-(L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = camalexin + hydrogen cyanide + CO2 + 2 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction);;(1a) 2-(L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (R)-dihydrocamalexate + hydrogen cyanide + [oxidized NADPH—hemoprotein reductase] + 2 H2O;;(1b) (R)-dihydrocamalexate + [reduced NADPH—hemoprotein reductase] + O2 = camalexin + CO2 + [oxidized NADPH—hemoprotein reductase] + 2 H2O
Other name(s)
CYP71B15 (gene name),
bifunctional dihydrocamalexate synthase/camalexin synthase
Systematic name
2-(cystein-S-yl)-2-(1H-indol-3-yl)-acetonitrile, [reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (camalexin-forming)
Comment
This cytochrome P-450 (heme thiolate) enzyme, which has been characterized from the plant Arabidopsis thaliana, catalyses the last two steps in the biosynthesis of camalexin, the main phytoalexin in that plant. The enzyme catalyses two successive oxidation events. During the first oxidation the enzyme introduces a C-N double bond, liberating hydrogen cyanide, and during the second oxidation it catalyses a decarboxylation.
History
created 2017
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000 1.14.99.6 created 1972, modified 2000, deleted 2000 1.14.99.8 created 1972, deleted 1984 1.14.99.13 created 1972, deleted 1984 1.14.99.16 created 1972, deleted 2002 1.14.99.17 created 1972, deleted 1976 1.14.99.18 created 1976, modified 1999, deleted 2003 1.14.99.25 created 1986, deleted 2000
