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Страница 1 от 35 полученные результаты
The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.
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The heme thiolate protein cytochrome P450tyr is a multifunctional N-hydroxylase converting L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (Sibbesen et al. (1995) J. Biol. Chem. 270, 3506-3511). Using a polyclonal antibody
Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase.
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A stable activity which transfers the amino group from glutamate to prephenate was extracted from 4-day old etiolated shoots of sorghum. The activity was retained on DEAE cellulose and eluted as a single peak. Prephenate aminotransferase co-eluted with a very abundant alpha-ketoglutarate: aspartate
Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase.
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The conversion of prephenic acid to tyrosine can occur by two different routes: (a) oxidative decarboxylation (prephenate dehydrogenase) followed by transamination (aromatic aminotransferase); (b) transamination of prephenate forming the non-aromatic amino acid arogenic acid (prephenate
Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.
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Cytochrome P-450TYR, which catalyzes the N-hydroxylation of L-tyrosine in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench has recently been isolated (Sibbesen, O., Koch, B., Halkier, B. A., and Møller, B. L. (1994) Proc. Natl. Acad. Sci. U.S.A. 92, 9740-9744).
Biochemical characterization of the major sorghum grain peroxidase.
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The major cationic peroxidase in sorghum grain (SPC4) , which is ubiquitously present in all sorghum varieties was purified to apparent homogeneity, and found to be a highly basic protein (pI approximately 11). MS analysis showed that SPC4 consists of two glycoforms with molecular masses of 34,227
Ileal amino acids digestibility of sorghum in weaned piglets and growing pigs.
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The objective of the study was to determine the coefficients of ileal apparent digestibility (CIAD) of sorghum protein and amino acids (AA) in weaned piglets and growing pigs. Digestibility coefficients were estimated using the regression and difference methods for the weaned piglets; and the direct
Flaked sorghum biscuits increase postprandial GLP-1 and GIP levels and extend subjective satiety in healthy subjects.
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Sorghum grain components may play a role in mechanisms that protect against development of obesity-related chronic diseases. We conducted a randomized, cross-over trial (40 healthy subjects) using whole grain sorghum flaked biscuits to investigate mechanisms related to satiety.
Subjects were tested
Influence of Sorghum Kafirin on Serum Lipid Profile and Antioxidant Activity in Hyperlipidemic Rats (In Vitro and In Vivo Studies).
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The aim of this study was to compare in vitro the antioxidant potential of sorghum kafirin and sorghum flour and their influence on lipids and antioxidant capacity in rats. The antioxidant activity in sorghum kafirin extract measured by the DPPH and TEAC methods was increased 30 and 65 times,
A monophenol oxidase activity in extracts of sorghum.
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A p-hydroxycinnamic acid oxidase activity was present in enzyme preparations from first internodes of Sorghum vulgare variety Wheatland milo when incubated in phosphate buffer at pH 7.5. This preparation had no classical polyphenolase activity but had both peroxidase and catalase activities. Since
Metabolic engineering of p-hydroxybenzylglucosinolate in Arabidopsis by expression of the cyanogenic CYP79A1 from Sorghum bicolor.
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Glucosinolates are natural products in cruciferous plants, including Arabidopsis thaliana. CYP79A1 is the cytochrome P450 catalysing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum. Both glucosinolates and cyanogenic
Accumulation of Carboxylate and Aromatic Fluorophores by a Pest-Resistant Sweet Sorghum [Sorghum bicolor (L.) Moench] Genotype.
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The sugary juice from sweet sorghum [Sorghum bicolor (L.) Moench] stalks can be used to produce edible syrup, biofuels, or bio-based chemical feedstock. The current cultivars are highly susceptible to damage from sugarcane aphids [Melanaphis sacchari (Zehntner)], but development of new
The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor.
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A microsomal fraction from seedlings of Sorghum bicolor (Linn) Moench has been shown to catalyze the conversion of L-tyrosine to p-hydroxymandelonitrile via p-hydroxyphenylacetaldoxime. This transformation is consistent with the general pathway for cyanogenic glycoside biosynthesis proposed on the
Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench.
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Arogenate dehydratase was purified sixfold from an extract of etiolated seedlings of Sorghum bicolor. Prephenate dehydratase was not detected. The arogenate dehydratase activity displayed hyperbolic substrate kinetics with a KM for arogenate of 0.32 mM. Activity was inhibited competitively by
Chorismate mutase isoenzymes from Sorghum bicolor: purification and properties.
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Two forms of chorismate mutase (EC 5.4.99.5), designated as CM-1 and CM-2, have been detected in etiolated seedlings of Sorghum bicolor after DEAE-cellulose chromatography. CM-1 and CM-2 contained 44 and 56%, respectively, of the total activity measured after DEAE-cellulose chromatography. CM-1 was
Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.
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The two multifunctional cytochrome P450 enzymes, CYP79A1 and CYP71E1, involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench have been characterized with respect to substrate specificity and cofactor requirements using reconstituted, recombinant enzymes and
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