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beta cyanoalanine/glycine max

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Treatment of etiolated seedlings of barley (Hordeum vulgare) and soybean (Glycine max) with 1 millimolar 2,4-dichlorophenoxyacetic acid (2,4-D) resulted in a 14-fold and greater than 100-fold increase in ethylene production, respectively. Simultaneous monitoring of endogenous cyanide and

Structure of soybean β-cyanoalanine synthase and the molecular basis for cyanide detoxification in plants.

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Plants produce cyanide (CN-) during ethylene biosynthesis in the mitochondria and require β-cyanoalanine synthase (CAS) for CN- detoxification. Recent studies show that CAS is a member of the β-substituted alanine synthase (BSAS) family, which also includes the Cys biosynthesis enzyme O-acetylserine

Assessing functional diversity in the soybean β-substituted alanine synthase enzyme family.

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In plants, proteins of the β-substituted alanine synthase (BSAS) enzyme family perform a diverse range of reactions, including formation of cysteine from O-acetylserine and sulfide, detoxification of cyanide by its addition to cysteine, the breakdown of cysteine into pyruvate, ammonia, and sulfide,

A role for ethylene in the metabolism of cyanide by higher plants.

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The action of ethylene on the capacity of plant tissues to metabolize cyanide to beta-cyanoalanine was examined. Beta-cyanoalanine synthase (EC 4.4.1.9) catalyzes the reaction between cyanide and cysteine to form beta-cyanoalanine and hydrogen sulfide. Levels of beta-cyanoalanine synthase activity

A possible new mechanism involved in ferro-cyanide metabolism by plants.

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OBJECTIVE Ferro-cyanide is one of the commonly found species at cyanide-contaminated soils and groundwater. Unlike botanical metabolism of KCN via the β-cyanoalanine pathway, processes involved in the plant-mediated assimilation of ferro-cyanide are still unclear. The objective of this study was to
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