Effect of Inhibitors of Pyridoxal-5′-Phosphate-Dependent Enzymes on Cysteine Synthase in Echinochloa crus-galli L.

Hirase, Kangetsu; Molin, William T.

doi:10.1006/pest.2001.2553

Cited by 7 publications

(5 citation statements)

References 23 publications

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“…These two compounds inhibited shoot growth of barnyardgrass in a whole‐plant bioassay. In the same experiment, allylglycine, β‐chloroalanine and 3‐bromopropionate slightly inhibited CS and had low phytotoxicity in vivo (Hirase & Molin 2001b).…”

Section: Potential Target Site For Herbicides On Sulfur Assimilation mentioning

confidence: 94%

“…Because CS requires PLP as a cofactor, the effect of inhibitors of PLP dependent enzymes on CS was examined. Amino‐oxyacetate (AOA) and hydroxylamine, non‐specific inhibitors of PLP‐dependent enzymes, inhibited CS extracted from leaves of barnyardgrass ( Echinochloa crus‐galli L.), and the degree of inhibition increased with the incubation period of the enzyme and inhibitors (Hirase & Molin 2001a, 2001b). These two compounds inhibited shoot growth of barnyardgrass in a whole‐plant bioassay.…”

Section: Potential Target Site For Herbicides On Sulfur Assimilation mentioning

confidence: 99%

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Sulfur assimilation in plants and weed control: Potential targets for novel herbicides and action sites of certain safeners

Hirase¹,

Molin²

2003

Weed Biology and Management

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Sulfur is an indispensable element for plants. It is found in sulfur-containing amino acids, cysteine and methionine, and in various other important biochemical components and processes. Inhibitors of sulfur assimilation, or cysteine and methionine synthesis, could be potential herbicides. In the present paper, the sulfur assimilation pathway in plants is described, followed by the introduction of several compounds (inhibitors and safeners) acting on this pathway. Uptake of inorganic sulfate through the roots is the first step of sulfur assimilation in plants. Sulfate is reduced mainly in chloroplasts to sulfide by a multistep process, and sulfide is then incorporated into cysteine. Cysteine is converted to cystathionine, homocysteine and methionine. Cysteine is incorporated into glutathione (GSH) by g -glutamylcysteine synthetase and GSH synthetase. Three enzymes involved in cysteine and methionine biosynthesis, cysteine synthase, cystathionine g -synthase and cystathionine b -lyase, have been investigated as target sites for herbicides. Several inhibitors of these enzymes (e.g. rhizobitoxine and propargylglycine) were also phytotoxic, suggesting that the synthetic pathway of sulfur-containing amino acids could be a new target site for herbicides. Some safeners for herbicides were found to act on the sulfur assimilation pathway and on GSH synthesis to increase GSH, which can be involved in herbicide metabolism and detoxification. Several safeners elevate GSH levels by increasing the activities of enzymes involved in sulfur assimilation and GSH synthesis. Further studies on plant sulfur metabolism may lead to the discovery of new herbicides and to the comprehensive understanding of the mode of action of safeners.

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Section: Potential Target Site For Herbicides On Sulfur Assimilation mentioning

confidence: 94%

Section: Potential Target Site For Herbicides On Sulfur Assimilation mentioning

confidence: 99%

Sulfur assimilation in plants and weed control: Potential targets for novel herbicides and action sites of certain safeners

Hirase¹,

Molin²

2003

Weed Biology and Management

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“…Several inhibitors of PLP-dependent enzymes were tested for inhibitory activity against CS from the leaves of Echinochloa crus-galli [345,346]. Preincubation with DL-allylglycine, DLpropargylglycine, β-chloro-L-alanine, 3-bromopropionate, amino-oxyacetate, hydroxylamine and cycloserine, at concentrations in the millimolar range, inhibited the CS activity.…”

Section: Cystathionine -Synthasementioning

confidence: 99%

Pyridoxal 5-Phosphate Enzymes as Targets for Therapeutic Agents

Amadasi¹,

Bertoldi²,

Contestabile³

et al. 2007

CMC

176

153

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The vitamin B(6)-derived pyridoxal 5'-phosphate (PLP) is the cofactor of enzymes catalyzing a large variety of chemical reactions mainly involved in amino acid metabolism. These enzymes have been divided in five families and fold types on the basis of evolutionary relationships and protein structural organization. Almost 1.5% of all genes in prokaryotes code for PLP-dependent enzymes, whereas the percentage is substantially lower in eukaryotes. Although about 4% of enzyme-catalyzed reactions catalogued by the Enzyme Commission are PLP-dependent, only a few enzymes are targets of approved drugs and about twenty are recognised as potential targets for drugs or herbicides. PLP-dependent enzymes for which there are already commercially available drugs are DOPA decarboxylase (involved in the Parkinson disease), GABA aminotransferase (epilepsy), serine hydroxymethyltransferase (tumors and malaria), ornithine decarboxylase (African sleeping sickness and, potentially, tumors), alanine racemase (antibacterial agents), and human cytosolic branched-chain aminotransferase (pathological states associated to the GABA/glutamate equilibrium concentrations). Within each family or metabolic pathway, the enzymes for which drugs have been already approved for clinical use are discussed first, reporting the enzyme structure, the catalytic mechanism, the mechanism of enzyme inactivation or modulation by substrate-like or transition state-like drugs, and on-going research for increasing specificity and decreasing side-effects. Then, PLP-dependent enzymes that have been recently characterized and proposed as drug targets are reported. Finally, the relevance of recent genomic analysis of PLP-dependent enzymes for the selection of drug targets is discussed.

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“…The resulting supernatant was used for the CS assay. The CS assay (26)(27)(28) was performed in a final volume of 1 ml containing 50 mM phosphate buffer, pH 7.8, less than 0.02 mg protein, 5 mM OAS, 1 mM Na2S, 1 mM dithiothreitol, 0.025 mM pyridoxal-5'phosphate. The substrates were added to the enzyme to initiate the reaction, and assay test tubes were sealed with rubber caps.…”

Section: Cs Assaymentioning

confidence: 99%

Effect of Flurazole and Other Safeners for Chloroacetanilide Herbicides on Cysteine Synthase in Sorghum Shoots

Hirase¹,

Molin²

2001

Pesticide Biochemistry and Physiology

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Effect of Inhibitors of Pyridoxal-5′-Phosphate-Dependent Enzymes on Cysteine Synthase in Echinochloa crus-galli L.

Cited by 7 publications

References 23 publications

Sulfur assimilation in plants and weed control: Potential targets for novel herbicides and action sites of certain safeners

Sulfur assimilation in plants and weed control: Potential targets for novel herbicides and action sites of certain safeners

Pyridoxal 5-Phosphate Enzymes as Targets for Therapeutic Agents

Effect of Flurazole and Other Safeners for Chloroacetanilide Herbicides on Cysteine Synthase in Sorghum Shoots

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