Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis.

Plant physiology - 1 Sept 2003

Naur Peter, Petersen Bent Larsen, Mikkelsen Michael Dalgaard, Bak Søren, Rasmussen Hasse, Olsen Carl Erik, Halkier Barbara Ann

Abstract excerpt

In the glucosinolate pathway, the postoxime enzymes have been proposed to have low specificity for the side chain and high specificity for the functional group. Here, we provide biochemical evidence for the functional role of the two cytochromes P450, CYP83A1 and CYP83B1, from Arabidopsis in oxim...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arabidopsis Proteins
Share to Cytochrome P-450 Enzyme System
Share to Glucosinolates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mixed Function Oxygenases

Share to Oximes

Share to Oxygenases

Share to Plants, Genetically Modified

Share to Reverse Transcriptase Polymerase Chain Reaction

Source

Open in PubMed Open full text

Identifiers

PMID: 12970475
DOI: 10.1104/pp.102.019240
PMCID: PMC196579

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12970475-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis.PMID 12970475Read ↗

CYP83b1 is the oxime-metabolizing enzyme in the glucosinolate pathway in Arabidopsis.Semantic proximity Read ↗

CYP79F1 and CYP79F2 have distinct functions in the biosynthesis of aliphatic glucosinolates in Arabidopsis.Semantic proximity Read ↗

Controlled indole-3-acetaldoxime production through ethanol-induced expression of CYP79B2.Semantic proximity Read ↗

The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways.Semantic proximity Read ↗

CYP83A1 is required for metabolic compatibility of Arabidopsis with the adapted powdery mildew fungus Erysiphe cruciferarum.Semantic proximity Read ↗

A glucosinolate metabolism pathway in living plant cells mediates broad-spectrum antifungal defense.Semantic proximity Read ↗

Bus, a bushy Arabidopsis CYP79F1 knockout mutant with abolished synthesis of short-chain aliphatic glucosinolates.Semantic proximity Read ↗

The Arabidopsis ref2 mutant is defective in the gene encoding CYP83A1 and shows both phenylpropanoid and glucosinolate phenotypes.Semantic proximity Read ↗

Metabolic engineering in Nicotiana benthamiana reveals key enzyme functions in Arabidopsis indole glucosinolate modification.Semantic proximity Read ↗

Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis.Semantic proximity Read ↗

A coumaroyl-ester-3-hydroxylase insertion mutant reveals the existence of nonredundant meta-hydroxylation pathways and essential roles for phenolic precursors in cell expansion and plant growth.Semantic proximity Read ↗

New nodes and edges in the glucosinolate molecular network revealed by proteomics and metabolomics of Arabidopsis myb28/29 and cyp79B2/B3 glucosinolate mutants.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.