KEGG ENZYME: 1.14.14.156

ENZYME: 1.14.14.156

Entry

EC 1.14.14.156              Enzyme

Name

tryptophan N-monooxygenase;
tryptophan N-hydroxylase;
CYP79B1;
CYP79B2;
CYP79B3

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

Sysname

L-tryptophan,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)

Reaction(IUBMB)

L-tryptophan + 2 [reduced NADPH---hemoprotein reductase] + 2 O2 = (E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH---hemoprotein reductase] + CO2 + 3 H2O (overall reaction) [RN:R08160];
(1a) L-tryptophan + [reduced NADPH---hemoprotein reductase] + O2 = N-hydroxy-L-tryptophan + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R09583];
(1b) N-hydroxy-L-tryptophan + [reduced NADPH---hemoprotein reductase] + O2 = N,N-dihydroxy-L-tryptophan + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R09584];
(1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O [RN:R09585]

Reaction(KEGG)

R08160 R09583 R09584 R09585

Substrate

L-tryptophan [CPD:C00078];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007];
N-hydroxy-L-tryptophan [CPD:C19716];
N,N-dihydroxy-L-tryptophan [CPD:C19717]

Product

(E)-indol-3-ylacetaldoxime [CPD:C02937];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
CO2 [CPD:C00011];
H2O [CPD:C00001];
N-hydroxy-L-tryptophan [CPD:C19716];
N,N-dihydroxy-L-tryptophan [CPD:C19717]

Comment

A cytochrome P-450 (heme-thiolate) protein from the plant Arabidopsis thaliana. This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.

History

EC 1.14.14.156 created 2011 as EC 1.14.13.125, transferred 2018 to EC 1.14.14.156

Pathway

ec00380

Tryptophan metabolism

ec00966

Glucosinolate biosynthesis

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K11812

tryptophan N-monooxygenase

K11813

tryptophan N-monooxygenase

Genes

ATH:	AT2G22330(CYP79B3) AT4G39950(CYP79B2)

ALY:	9302968 9314677

CRB:	17879334 17889834

CSAT:

104702772 104713678 104716281 104720922 104729322 104729349 104751874

EUS:	EUTSA_v10000114mg EUTSA_v10000278mg EUTSA_v10024861mg

BRP:	103835554 103853878 103862605 103864341

BNA:	106361376 106382592 106410467 106439341 106441279 106446405 125580497 125584456

BOE:	106301717 106302779 106330945 106337668

RSZ:	108818790 108819835 108830725 108854183 108855674 130507033 130507293 130507697 130511890

THJ:	104804164 104807687 104824879

TDC:	119320796 119348157

» show all

Reference

1 [PMID:10922360]

Authors

Mikkelsen MD, Hansen CH, Wittstock U, Halkier BA

Title

Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid.

Journal

J Biol Chem 275:33712-7 (2000)
DOI:10.1074/jbc.M001667200

Sequence

[ath:AT4G39950]

Reference

2 [PMID:10681464]

Authors

Hull AK, Vij R, Celenza JL

Title

Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis.

Journal

Proc Natl Acad Sci U S A 97:2379-84 (2000)
DOI:10.1073/pnas.040569997