Biosynthesis of ethylene. Methanesulphinic acid as cofactor in the enzymic formation of ethylene from methional

Mapson, L. W.; Self, Ron; Wardale, D. A.

doi:10.1042/bj1110413

Cited by 14 publications

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“…These enzymes have since been identified as a glucose oxidase and a peroxidase ). The peroxidase utilizes the hydrogen peroxide produced by the oxidase to convert the C-3 and C-4 atoms of methional into ethylene in the presence of two cofactors, a phenolic acid and a sulphinic acid (Mapson & Mead, 1968;Mapson, Self & Wardale, 1969). In the earlier work, we also showed the necessity for the synthesis from methionine of an enzyme present in the mitochondrial-microsomal fraction, and suggested that the function of this enzyme in the synthetic pathW way was to produce a precursor similar to or identical with methional.…”

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Biosynthesis of ethylene. 4-Methylmercapto-2-oxobutyric acid, an intermediate in the formation from methionine

Mapson

March

Wardale

1969

Biochemical Journal

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The enzyme responsible for the conversion of methionine into a precursor of ethylene in cauliflower florets is a transaminase. The formation of 4-methyl-mercapto-2-oxobutyric acid by this enzyme has been shown. The oxo acid stimulates the synthesis of ethylene when added to floret tissue, and tracer experiments have shown that (14)C is incorporated into ethylene from the labelled oxo acid. The evidence is consistent with the view that the oxo acid is an intermediate in the formation of ethylene from methionine.

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Biosynthesis of ethylene. 4-Methylmercapto-2-oxobutyric acid, an intermediate in the formation from methionine

Mapson

March

Wardale

1969

Biochemical Journal

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“…was added to start the reaction, and the ethylene concentration was determined with a gas chromatograph after 5-min incubation at room temperature. In experiments with crystallized egg albumin, 12 (21) containing MnSO4, resorcinol, NaHSO, KH2P04 (pH 7.8), and horseradish peroxidase was used to measure ethylene production from various concentrations of substrates after 5-min incubation. The initial rates of ethylene evolution were calculated by substracting the rate of the complete system without peroxidase from the rate of the complete system.…”

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Ethylene Production from Peptides and Protein Containing Methionine

Demorest

Stahmann

1971

Plant Physiol.

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It has been reported that the C0-C4 carbons of methionine are converted to ethylene in and Cu"!-ascorbate (10) model systems. Yang (22) has shown that C-C, carbons of 2-keto-4-methylthiobutyrate and the Cr, carbons of 3-methylthiopropionaldehyde (i.e., methional) are converted to ethylene in a model peroxidase system. When methionine was fed to apple tissue, the C-C4 carbons were apparently converted to ethylene (1,11). These reports demonstrate that the CrCa carbons of methionine or its related derivatives are converted to ethylene in model systems and in plant tissue. It was thus of interest to demonstrate whether or not methionine residues in protein and peptides could be converted to ethylene. Using a peroxidase system described by Yang (21), it was found that peptides containing a C-terminal methionine residue, but not an N-terminal or internal residue, produced ethylene at initial rates two to four times greater than the small but significant rate from methionine. Purified egg albumin did not produce any ethylene; however, after limited proteolysis of egg albumin, significant ethylene was formed. Of particular importance was the finding that N-acetyl-D,L-methionine produced ethylene at a rate about equal to methional.The methods used were similar to those described by Yang (21). The incubation mixture contained the following in a total volume of 1 ml: 0.05 ,mole of MnSO4, 0.02 ,umole of resorcinol, 50 imoles of KH,PO, (pH 7.8), 3.0 ,ug of peroxidase, 2.0 umoles of NaHSO., and 0.5, 1.0, or 2.0 ,umoles of substrate. The NaHSO. was added to start the reaction, and the ethylene concentration was determined with a gas chromatograph after 5-min incubation at room temperature. In experiments with crystallized egg albumin, 12 umoles of H110, was substituted for the MnSO,.

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Biosynthesis and Metabolism of Plant Hormones

Sembdner¹,

Gross²,

Liebisch³

et al. 1980

Hormonal Regulation of Development I

132

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Biosynthesis of ethylene. Methanesulphinic acid as cofactor in the enzymic formation of ethylene from methional

Abstract: The second cofactor in the peroxidase-catalysed formation of ethylene from methional in cauliflower extracts was identified as methanesulphinic acid. The progress of the reaction is described and the activities of related sulphinic acids were determined.

Cited by 14 publications

References 13 publications

Biosynthesis of ethylene. 4-Methylmercapto-2-oxobutyric acid, an intermediate in the formation from methionine

Biosynthesis of ethylene. 4-Methylmercapto-2-oxobutyric acid, an intermediate in the formation from methionine

Ethylene Production from Peptides and Protein Containing Methionine

Biosynthesis and Metabolism of Plant Hormones

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