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triglochin concinna/7 glucoside
Veza se sprema u međuspremnik
6 rezultatima
Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima.
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Two cDNA clones encoding cytochrome P450 enzymes belonging to the CYP79 family have been isolated from Triglochin maritima. The two proteins show 94% sequence identity and have been designated CYP79E1 and CYP79E2. Heterologous expression of the native and the truncated forms of the two clones in
Biosynthesis of cyanogenic glucosides in Triglochin maritima and the involvement of cytochrome P450 enzymes.
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The biosynthesis of the two cyanogenic glucosides, taxiphyllin and triglochinin, in Triglochin maritima (seaside arrow grass) has been studied using undialyzed microsomal preparations from flowers and fruits. Tyrosine was converted to p-hydroxymandelonitrile with V(max) and K(m) values of 36 nmol
Biosynthesis of cyanogenic glucosides: in vitro analysis of the glucosylation step.
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The last step in the biosynthesis of cyanogenic glucosides, the glucosylation of the cyanohydrin intermediate, has been investigated in detail using Triglochin maritima seedlings. The glucosyltransferase activity is not associated with membranes and appears to be a "soluble" enzyme. The cyanohydrin
Aspects on the Biosynthesis of the Cyanogenic Glucoside Triglochinin in Triglochin maritima1.
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The incorporation of L-[U- (14)C]phenylalanine, L-[U- (14)C]tyrosine and [U- (14)C]4-hydroxyphenylacetonitrile into triglochinin and taxiphyllin, the latter a possible precursor of the former, was studied in seedlings of TRIGLOCHIN MARITIMA L. The nitrile was by far the best substrate; incorporation
In vitro biosynthesis of the cyanogenic glucoside taxiphyllin in Triglochin maritima.
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The in vitro biosynthesis of taxiphyllin and the channeling of intermediates in Triglochin maritima.
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The in vitro biosynthesis of the cyanogenic glucoside taxiphyllin has recently been demonstrated in Triglochin maritima (Hösel, W., and Nahrstedt, A. (1980) Arch. Biochem. Biophys. 203, 753-757). We have now studied in more detail the multistep conversion of tyrosine into p-hydroxymandelonitrile,
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