mandelonitrile/sorgo

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Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.).

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(S)-p-Hydroxy-mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging-drop vapor-diffusion technique. Crystal form I is obtained from 1.4 M (NH(4))(2)SO(4) in 100 mM Na-acetate, pH 4.6, and belongs to the orthorhombic space group P2(1)2(1)2(1). The

Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases.

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Plant beta-glucosidases display varying substrate specificities. The maize beta-glucosidase isozyme Glu1 (ZmGlu1) hydrolyzes a broad spectrum of substrates in addition to its natural substrate DIMBOA-Glc (2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxaxin-3-one), whereas the sorghum

The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor.

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The in vitro substrate specificity of UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase from Sorghum bicolor (UGT85B1) was examined using a range of potential acceptor molecules, including cyanohydrins, terpenoids, phenolics, hexanol derivatives and plant hormones. Qualitative enzyme

Localization of Cinnamic Acid 4-Monooxygenase and the Membrane-bound Enzyme System for Dhurrin Biosynthesis in Sorghum Seedlings.

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The localization of three monooxygenase (hydroxylase) enzyme systems which occur in dark-grown seedlings of Sorghum bicolor has been studied. Cinnamic acid 4-hydroxylase (CAH) (trans-cinnamate 4-monooxygenase, EC 1.14.13.11), which has been increasingly utilized in plants as a marker for the

Leakage of Dhurrin and p-Hydroxybenzaldehyde from Young Sorghum Shoots Immersed in Various Solvents.

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Spectral scanning was used to provide estimates of the leakage of the cyanogenic glucoside, dhurrin (p-hydroxy-[S]-mandelonitrile-beta-d-glucoside), and its metabolite, p-hydroxybenzaldehyde (p-HB), from young light-grown shoots of Atlas sorghum (Sorghum bicolor [L.] Moench) when these shoots were

Subcellular Localization of Dhurrin beta-Glucosidase and Hydroxynitrile Lyase in the Mesophyll Cells of Sorghum Leaf Blades.

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Studies with purified mesophyll and epidermal protoplasts and bundle sheath strands have shown that the cyanogenic glucoside dhurrin (p-hydroxy-(S)-mandelonitrile-beta-d-glucoside) is localized in the epidermis of sorghum leaves whereas the enzymes involved in its degradation (dhurrin

Characterization of beta-glucosidases with high specificity for the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) moench seedlings.

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Two beta-glucosidases exhibiting high specificity for the cyanogenic glucoside dhurrin have been purified to near homogeneity from seedlings of Sorghum bicolor. Dhurrinase 1 was isolated from shoots of seedlings grown in the dark. Dhurrinase 2 was isolated from the green shoots of young seedlings

The aglycone specificity-determining sites are different in 2, 4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (Maize beta -glucosidase) and dhurrinase (Sorghum beta -glucosidase).

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The maize beta-glucosidase isozyme Glu1 hydrolyzes a broad spectrum of substrates in addition to its natural substrate DIMBOAGlc (2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-on e), whereas the sorghum beta-glucosidase isozyme Dhr1 hydrolyzes exclusively its natural substrate

Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate.

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Plant beta-glucosidases play a crucial role in defense against pests. They cleave, with variable specificity, beta-glucosides to release toxic aglycone moieties. The Sorghum bicolor beta-glucosidase isoenzyme Dhr1 has a strict specificity for its natural substrate dhurrin

Tissue Distributions of Dhurrin and of Enzymes Involved in Its Metabolism in Leaves of Sorghum bicolor.

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The tissue distributions of dhurrin [p-hydroxy-(S)-mandelonitrile-beta-d-glucoside] and of enzymes involved in its metabolism have been investigated in leaf blades of light-grown Sorghum bicolor seedlings. Enzymic digestion of these leaves using cellulase has enabled preparations of epidermal and

The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity.

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The final step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor is the transformation of the labile cyanohydrin into a stable storage form by O-glucosylation of (S)-p-hydroxymandelonitrile at the cyanohydrin function. The

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