KEGG   ENZYME: 1.14.14.45Help
Entry
EC 1.14.14.45               Enzyme                                 

Name
aromatic aldoxime N-monooxygenase;
CYP83B1 (gene name)
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
BRITE hierarchy
Sysname
(E)-indol-3-ylacetaldoxime,[reduced NADPH---hemoprotein reductase],glutathione:oxygen oxidoreductase (oxime-hydroxylating)
Reaction(IUBMB)
(1) (E)-indol-3-ylacetaldehyde oxime + [reduced NADPH---hemoprotein reductase] + glutathione + O2 = S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + [oxidized NADPH---hemoprotein reductase] + 2 H2O (overall reaction) [RN:R11734];
(1a) (E)-indol-3-ylacetaldehyde oxime + [reduced NADPH---hemoprotein reductase] + O2 = 1-(1H-indol-3-yl)-2-aci-nitroethane + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R11735];
(1b) 1-(1H-indol-3-yl)-2-aci-nitroethane + glutathione = S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + H2O (spontaneous) [RN:R11736];
(2) (E)-phenylacetaldehyde oxime + [reduced NADPH---hemoprotein reductase] + glutathione + O2 = S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + [oxidized NADPH---hemoprotein reductase] + 2 H2O (overall reaction) [RN:R11737];
(2a) (E)-phenylacetaldehyde oxime + [reduced NADPH---hemoprotein reductase] + O2 = 1-aci-nitro-2-phenylethane + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R11738];
(2b) 1-aci-nitro-2-phenylethane + glutathione = S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + H2O (spontaneous) [RN:R11739]
Reaction(KEGG)
Substrate
(E)-indol-3-ylacetaldehyde oxime;
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
glutathione [CPD:C00051];
O2 [CPD:C00007];
1-(1H-indol-3-yl)-2-aci-nitroethane [CPD:C17204];
(E)-phenylacetaldehyde oxime [CPD:C19714];
1-aci-nitro-2-phenylethane [CPD:C21623]
Product
S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione [CPD:C21620];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001];
1-(1H-indol-3-yl)-2-aci-nitroethane [CPD:C17204];
S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione [CPD:C21622];
1-aci-nitro-2-phenylethane [CPD:C21623]
Comment
This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of glucosinolates in plants. The enzyme catalyses the N-hydroxylation of aromatic aldoximes derived from L-tryptophan, L-phenylalanine, and L-tyrosine, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates. In the absence of glutathione, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro compound with catalytic residues in the active site.
History
EC 1.14.14.45 created 2017
Pathway
ec00380  Tryptophan metabolism
ec00966  Glucosinolate biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K11818  aromatic aldoxime N-monooxygenase
Genes
ATH: AT4G31500(CYP83B1)
ALY: ARALYDRAFT_913321
CRB: 17879907
CSAT: 104721689 104730102
EUS: EUTSA_v10004064mg
BRP: 103833295
BNA: 106361266 106372082
BOE: 106312180
RSZ: 108829823
THJ: 104806926
CPAP: 110818289
 » show all
Taxonomy
Reference
1  [PMID:11158532]
  Authors
Bak S, Tax FE, Feldmann KA, Galbraith DW, Feyereisen R
  Title
CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis.
  Journal
Plant Cell 13:101-11 (2001)
Reference
2  [PMID:12970475]
  Authors
Naur P, Petersen BL, Mikkelsen MD, Bak S, Rasmussen H, Olsen CE, Halkier BA.
  Title
CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis.
  Journal
Plant Physiol 133:63-72 (2003)
DOI:10.1104/pp.102.019240
Reference
3  [PMID:21712415]
  Authors
Geu-Flores F, Moldrup ME, Bottcher C, Olsen CE, Scheel D, Halkier BA
  Title
Cytosolic gamma-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis.
  Journal
Plant Cell 23:2456-69 (2011)
DOI:10.1105/tpc.111.083998
  Sequence
[ath:AT4G31500]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.45
IUBMB Enzyme Nomenclature: 1.14.14.45
ExPASy - ENZYME nomenclature database: 1.14.14.45
BRENDA, the Enzyme Database: 1.14.14.45

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