Gene Ontology annotation through association of InterPro records with GO terms
-
InterPro2GO maps FMO domain signatures to FAD binding, NADP binding (both correct) and to the mammalian N,N-dimethylaniline monooxygenase activity, which is not supported for this glucosinolate-specific plant enzyme (MODIFY).
Annotation inferences using phylogenetic trees
Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis.
-
Identifies FMO GS-OX1 as the enzyme converting methylthioalkyl to methylsulfinylalkyl glucosinolates, by recombinant enzyme assays, overexpression (near-complete conversion; ~5-fold more 4-methylsulfinylbutyl glucosinolate in seeds) and knockout analysis.
"We report the identification of an Arabidopsis flavin-monooxygenase (FMO) enzyme, FMO(GS-OX1), which catalyzes the conversion of methylthioalkyl GSLs into methylsulfinylalkyl GSLs."
Subclade of flavin-monooxygenases involved in aliphatic glucosinolate biosynthesis.
-
Defines the crucifer-specific FMO GS-OX1-5 subclade; FMO GS-OX1-4 have broad chain-length specificity (4-MTB and 8-MTO), GS-OX5 is 8-MTO-specific; FMO GS-OX1 requires the S-glucosyl group of its substrate; FMO GS-OX1 and GS-OX2 control 8-MSO production in planta.
"Interestingly, all five recombinant proteins converted 8-MTO to 8-MSO"