KEGG   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)
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
CRB: 17879334 17889834
CSAT: 104716281 104720922 104729322 104729349 104751874
EUS: EUTSA_v10000114mg EUTSA_v10024861mg
BRP: 103853878 103862605 103864341
BNA: 106382592 106410467 106439341 106441279 106446405
BOE: 106301717 106302779 106330945 106337668
RSZ: 108818790 108830725 108851800 108855674
THJ: 104807687 104824879
CPAP: 110806501
 » 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
  Sequence
Reference
3  [PMID:12464638]
  Authors
Zhao Y, Hull AK, Gupta NR, Goss KA, Alonso J, Ecker JR, Normanly J, Chory J, Celenza JL
  Title
Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s  CYP79B2 and CYP79B3.
  Journal
Genes Dev 16:3100-12 (2002)
DOI:10.1101/gad.1035402
Reference
4  [PMID:12464264]
  Authors
Naur P, Hansen CH, Bak S, Hansen BG, Jensen NB, Nielsen HL, Halkier BA
  Title
CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime.
  Journal
Arch Biochem Biophys 409:235-41 (2003)
DOI:10.1016/S0003-9861(02)00567-2
  Sequence
[brp:103853878]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.156
IUBMB Enzyme Nomenclature: 1.14.14.156
ExPASy - ENZYME nomenclature database: 1.14.14.156
BRENDA, the Enzyme Database: 1.14.14.156

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