Properties and localization of the homoglutathione synthetase from <i>Phaseolus coccineus</i> leaves

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<jats:p>The synthesis of homoglutathione (hGSH) by several plants of the tribe Phaseoleae is shown to be catalysed by a β‐alanine‐specific hGSH synthetase, Properties of the enzyme from <jats:italic>Phaseolus coccineus</jats:italic> L. cv. Preisgewinner were studied, using ammonium sulfate precipitates of primary leaf extracts. The hGSH synthetase showed a broad pH optimum at pH 8–9, an absolute requirement for Mg<jats:sup>2+</jats:sup>, a stimulation by K<jats:sup>+</jats:sup>, and a high affinity for γ‐glutamylcysteine [K<jats:sub>m</jats:sub>(app.) 73 μ<jats:italic>M</jats:italic>]. The enzyme exhibited a high specificity for β‐alanine [K<jats:sub>m</jats:sub>(app.) 1.34 m<jats:italic>M</jats:italic>] compared to glycine [K<jats:sub>m</jats:sub>(app.) 98 m<jats:italic>M</jats:italic>]. Chloroplasts, isolated from the leaves of <jats:italic>Phaseolus coccineus</jats:italic>, contained about 17% of the hGSH synthetase activity in the leaf cells.</jats:p>

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