A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.
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The enzyme appears in viruses and cellular organisms
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
no substrate: L-leucine, L-phenylalanine, L-tyrosine. The observed substrate specificity corresponds with the in vivo presence of only L-valine- and L-isoleucine-derived cyanogenic glucosides in cassava
no substrate: L-leucine, L-phenylalanine, L-tyrosine. The observed substrate specificity corresponds with the in vivo presence of only L-valine- and L-isoleucine-derived cyanogenic glucosides in cassava
enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
CYP79D1 and CYP79D2 are the two paralogous genes encoding the first committed enzymes in linamarin and lotaustralin synthesis. Blocking expression by RNA interference results in lines with acyanogenic leaves. Only a few of these lines are depleted with respect to cyanogenic glucoside content in tubers. Cyanogenic glucosides are synthesized in the shoot apex and transported to the root, resulting in a negative concentration gradient basipetal in the plant with the concentration of cyanogenic glucosides being highest in the shoot apex and the petiole of the first unfolded leaf
in Lotus japonicus expressing Manihot esculenta CYP79D2, the the cyanide potential is approximately twice as high as in wild-type plants. While thelinamarin content is increased approximately 20fold, the lotaustralin content is only slightly increased. The ratio of rhodiocyanoside A and D to lotaustralin is unaltered in leaves. In roots expressing cassava CYP79D2, linamarin and lotaustralin can be detected although in much smaller quantities than in green tissue
transgenic plants in which the expression of CYP79D1/CYP79D2 genes is selectively inhibited in leaves by antisense expression of CYP79D1/D2 gene fragments have 60-94% reduced linamarin leaf levels. These plants also have a greater than a 99% reduction in root linamarin content. Transgenic plants in which the CYP79D1/D2 transcripts are reduced to non-detectable levels in roots have normal root linamarin levels. Linamarin synthesized in leaves is transported to the roots and accounts for nearly all of the root linamarin content. Transgenic plants having reduced leaf and root linamarin content are unable to grow in the absence of NH3
transgenic plants in which the expression of CYP79D1/D2 genes is selectively inhibited in leaves by antisense expression of CYP79D1/D2 gene fragments have 60-94% reduced linamarin leaf levels. These plants also have a greater than a 99% reduction in root linamarin content. Transgenic plants in which the CYP79D1/D2 transcripts are reduced to non-detectable levels in roots have normal root linamarin levels. Linamarin synthesized in leaves is transported to the roots and accounts for nearly all of the root linamarin content. Transgenic plants having reduced leaf and root linamarin content are unable to grow in the absence of NH3
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava. CYP79D1 has a higher kcat value with L-valine as substrate than with L-isoleucine, which is consistent with linamarin being the major cyanogenic glucoside in cassava
enzyme catalyzes the conversion of Val and Ile to the corresponding aldoximes in biosynthesis of cyanogenic glucosides and nitrile glucosides in Lotus japonicus. Recombinantly expressed isoforms CYP79D3 and CYP79D4 in yeast cells show higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
CYP79D1 and CYP79D2 are the two paralogous genes encoding the first committed enzymes in linamarin and lotaustralin synthesis. Blocking expression by RNA interference results in lines with acyanogenic leaves. Only a few of these lines are depleted with respect to cyanogenic glucoside content in tubers. Cyanogenic glucosides are synthesized in the shoot apex and transported to the root, resulting in a negative concentration gradient basipetal in the plant with the concentration of cyanogenic glucosides being highest in the shoot apex and the petiole of the first unfolded leaf
expression of CYP79D2 from cassava in Arabidopsis thaliana results in the production of valine- and isoleucine-derived glucosinolates not normally found in this ecotype. The transgenic lines show no morphological phenotype, and the level of endogenous glucosinolates is not affected. The novel glucosinolates constitute up to 35% of the total glucosinolate content in mature rosette leaves and up to 48% in old leaves. At increased concentrations of these glucosinolates, the proportion of Val-derived glucosinolates decreases. As the isothiocyanates produced from the Val- and isoleucine-derived glucosinolates are volatile, metabolically engineered plants producing these glucosinolates have acquired novel properties with great potential for improvement of resistance to herbivorous insects and for biofumigation
expression of CYP79D2 from cassava in Arabidopsis thaliana results in the production of valine- and isoleucine-derived glucosinolates not normally found in this ecotype. The transgenic lines show no morphological phenotype, and the level of endogenous glucosinolates is not affected. The novel glucosinolates constitute up to 35% of the total glucosinolate content in mature rosette leaves and up to 48% in old leaves. At increased concentrations of these glucosinolates, the proportion of Val-derived glucosinolates decreases. As the isothiocyanates produced from the Val- and isoleucine-derived glucosinolates are volatile, metabolically engineered plants producing these glucosinolates have acquired novel properties with great potential for improvement of resistance to herbivorous insects and for biofumigation
Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin: Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes
Cassava plants with a depleted cyanogenic glucoside content in leaves and tubers. Distribution of cyanogenic glucosides, their site of synthesis and transport, and blockage of the biosynthesis by RNA interference technology
Characterization and expression profile of two UDP-glucosyltransferases, UGT85K4 and UGT85K5, catalyzing the last step in cyanogenic glucoside biosynthesis in cassava