KEGG   ENZYME: 1.14.13.125Help
Entry
EC 1.14.13.125              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 NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
L-tryptophan,NADPH:oxygen oxidoreductase (N-hydroxylating)
Reaction(IUBMB)
L-tryptophan + 2 O2 + 2 NADPH + 2 H+ = (E)-indol-3-ylacetaldoxime + 2 NADP+ + CO2 + 3 H2O (overall reaction) [RN:R08160];
(1a) L-tryptophan + O2 + NADPH + H+ = N-hydroxy-L-tryptophan + NADP+ + H2O [RN:R09583];
(1b) N-hydroxy-L-tryptophan + O2 + NADPH + H+ = N,N-dihydroxy-L-tryptophan + NADP+ + H2O [RN:R09584];
(1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O [RN:R09585]
Reaction(KEGG)
Substrate
L-tryptophan [CPD:C00078];
O2 [CPD:C00007];
NADPH [CPD:C00005];
H+ [CPD:C00080];
N-hydroxy-L-tryptophan [CPD:C19716];
N,N-dihydroxy-L-tryptophan [CPD:C19717]
Product
(E)-indol-3-ylacetaldoxime [CPD:C02937];
NADP+ [CPD:C00006];
CO2 [CPD:C00011];
H2O [CPD:C00001];
N-hydroxy-L-tryptophan [CPD:C19716];
N,N-dihydroxy-L-tryptophan [CPD:C19717]
Comment
A heme-thiolate protein (P-450). 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 1.14.13.125 created 2011
Pathway
ec00380  Tryptophan metabolism
ec00966  Glucosinolate biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K11812  tryptophan N-monooxygenase
K11813  tryptophan N-monooxygenase
Genes
ATH: AT2G22330(CYP79B3) AT4G39950(CYP79B2)
ALY: ARALYDRAFT_481097 ARALYDRAFT_490780
CRB: 17879334 17889834
CSAT: 104729349 104751874
EUS: EUTSA_v10000114mg EUTSA_v10024861mg
BRP: 103853878(CYP79B1) 103862605(CYP79B2-2) 103864341(CYP79B3)
BNA: 106410467 106439341 106446405
BOE: 106301717 106302779 106330945 106337668
THJ: 104807687 104824879
HAN: 110877423 110924458
Taxonomy
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 (2000) 33712-7.
  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 (2000) 2379-84.
  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 (2002) 3100-12.
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 (2003) 235-41.
  Sequence
[brp:103853878]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.125
IUBMB Enzyme Nomenclature: 1.14.13.125
ExPASy - ENZYME nomenclature database: 1.14.13.125
BRENDA, the Enzyme Database: 1.14.13.125

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