EC number:1.14.14.43

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.14.43
Description:(Methylsulfanyl)alkanaldoxime N-monooxygenase.
Alternative Name: CYP83A1.
(Methylthio)alkanaldoxime N-monooxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.14.43
BRENDA Enzyme Link: BRENDA 1.14.14.43
KEGG Enzyme Link: KEGG1.14.14.43
BioCyc Enzyme Link: BioCyc 1.14.14.43
ExPASy Enzyme Link: ExPASy1.14.14.43
EC2PDB Enzyme Link: EC2PDB 1.14.14.43
ExplorEnz Enzyme Link: ExplorEnz 1.14.14.43
PRIAM enzyme-specific profiles Link: PRIAM 1.14.14.43
IntEnz Enzyme Link: IntEnz 1.14.14.43
MEDLINE Enzyme Link: MEDLINE 1.14.14.43

EC number:1.14.14.43

MSA:

1.14.14.43;
Phylogenetic Tree:

1.14.14.43;
Uniprot:
M-CSA:
RHEA:51992 an (E)-omega-(methylsulfanyl)-alkanal oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-glutathione + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[*:3]:[*:4]-[NH;+0:5]-[c;H0;+0:6](:[*:7]):[c;H0;+0:8]-1:[nH;+0:9]:[*:10].[*:11]-[SH;+0:12].[*:13]=[CH;+0:14]-[*:15].[O;H0;+0:16]=[O;H0;+0:17]>>[*:11]-[S;H0;+0:12]-[C;H0;+0:14](=[*:13])-[*:15].[*:1]-[n;H0;+0:2]1:[*:3]:[*:4]:[n;H0;+0:5]:[c;H0;+0:6](:[*:7])-[c;H0;+0:8]:1:[n;H0;+0:9]:[*:10].[OH2;+0:16].[OH2;+0:17]
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References

TitleAuthorsDatePubMed ID
CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis.Naur P, Petersen BL, Mikkelsen MD, Bak S, Rasmussen H, Olsen CE, Halkier BA2003 Sep12970475
CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis.Bak S, Tax FE, Feldmann KA, Galbraith DW, Feyereisen R2001 Jan11158532
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways.Clausen M, Kannangara RM, Olsen CE, Blomstedt CK, Gleadow RM, Jørgensen K, Bak S, Motawie MS, Møller BL2015 Nov26361733