Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
The involvement of two p450 enzymes, CYP83B1 and CYP83A1, in auxin homeostasis and glucosinolate biosynthesis.
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CYP83A1 and CYP83B1 both convert aldoximes to thiohydroximate adducts with NADPH and a thiol donor; indole-3-acetaldoxime is the physiological substrate of CYP83B1 but not CYP83A1, which acts on non-tryptophan aldoximes.
"Both enzymes convert indole-3-acetaldoxime to a thiohydroximate adduct in the presence of NADPH and a nucleophilic thiol donor."
The Arabidopsis ref2 mutant is defective in the gene encoding CYP83A1 and shows both phenylpropanoid and glucosinolate phenotypes.
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ref2 (cyp83a1) mutants have reduced levels of all aliphatic glucosinolates and increased indole glucosinolates.
"ref2 mutants were found to have reduced levels of all aliphatic glucosinolates and increased levels of indole-derived glucosinolates in their leaves"
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The phenylpropanoid (sinapate ester, syringyl lignin) phenotypes of ref2 are attributed to O-methyltransferase inhibition by accumulated aldoximes, i.e. an indirect effect.
"Instead, biochemical analysis of ref2 , and the inhibition of COMT by ref2 extracts in vitro, suggest that the phenylpropanoid phenotypes of the mutant may be attributable to the inhibition of O -methyltransferase activities by one or more aldoximes accumulated in the mutant"
CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis.
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Recombinant CYP83A1 efficiently metabolizes aliphatic methionine-derived oximes (Km about 20-150 uM) and forms glutathione conjugates; CYP83B1 does so poorly.
"we show that aliphatic oximes derived from chain-elongated homologs of methionine are efficiently metabolized by CYP83A1, whereas CYP83B1 metabolizes these substrates with very low efficiency."
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CYP83A1 and CYP83B1 are non-redundant in planta.
"The data show that CYP83A1 and CYP83B1 are nonredundant enzymes under physiologically normal conditions in the plant."
Water stress and aphid feeding differentially influence metabolite composition in Arabidopsis thaliana (L.).
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Aphid infestation decreased CYP83A1 transcripts.
"transcript levels of biosynthetic genes MAM1, CYP79F1, CYP83A1, and UGT74C1 decreased after infestation with either aphid species"
Global Analysis of Membrane-associated Protein Oligomerization Using Protein Correlation Profiling.
UniProtKB entry P48421 (CYP83A1)