This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-phenylalanine, a committed step in the biosynthesis of benzylglucosinolate and the cyanogenic glucosides (R)-prunasin and (R)-amygdalin. The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is labile and undergoes dehydration followed by decarboxylation, producing an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.
This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-phenylalanine, a committed step in the biosynthesis of benzylglucosinolate and the cyanogenic glucosides (R)-prunasin and (R)-amygdalin. The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is labile and undergoes dehydration followed by decarboxylation, producing an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.
CYP83B1 catalyzes the conversion of the (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate with retention of the configuration of the E-oxime intermediate in the final glucosinolate core structure. CYP83B1 from Arabidopsis thaliana cannot convert the (E)-p-hydroxyphenylacetaldoxime to the (Z)-isomer, which blocks the route towards cyanogenic glucoside synthesis
CYP83B1 catalyzes the conversion of the (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate with retention of the configuration of the E-oxime intermediate in the final glucosinolate core structure. CYP83B1 from Arabidopsis thaliana cannot convert the (E)-p-hydroxyphenylacetaldoxime to the (Z)-isomer, which blocks the route towards cyanogenic glucoside synthesis
expressed specifically in the seedling, coexpression with CYP71AN24 which catalyzes the conversion of phenylacetaldoxime into mandelonitrile with broad substrate specificity
enzyme is an N-hydroxylase converting L-phenylalanine into phenylacetaldoxime, the precursor of benzylglucosinolate. Transgenic Arabidopsis thaliana constitutively expressing CYP79A2 accumulate high levels of benzylglucosinolate
biosynthetic pathway for the production of phenylacetonitrile in Escherichia coli utilizing enzymes from the plant glucosinolate-biosynthetic and bacterial aldoxime-nitrile pathways, i.e. introducing the genes encoding cytochrome P450 (CYP) 79A2 and CYP reductase from Arabidopsis thaliana, yielding the E,Z-phenylacetaldoxime-producing transformant and further introducing the aldoxime dehydratase (Oxd) gene from Bacillus sp. strain OxB-1, yielding the phenylacetonitrile-producing transformant. Expression of active CYP79A2 and concentration of biomass are improved by the combination of the autoinduction method, coexpression of groE, encoding the heat shock protein GroEL/GroES, N-terminal truncation of CYP79A2, and optimization of the culture conditions, yielding a more than 60fold concentration of E,Z-phenylacetaldoxime up to 2.9 mM
Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. catalyzes the conversion of L-phenylalanine to phenylacetaldoxime in the biosynthesis of benzylglucosinolate
Construction of the biosynthetic pathway for the cyanide-free production of phenylacetonitrile in Escherichia coli utilizing plant cytochrome P450 79A2 and bacterial aldoxime dehydratase
Identification and characterization of CYP79D16 and CYP71AN24 catalyzing the first and second steps in L-phenylalanine-derived cyanogenic glycoside biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc