Acetolactate and Acetoin Synthesis in Ripening Peas

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Abstract
Ammonium sulphate fractionated extracts of ripening pea seeds contained 2 enzymes capable of synthesizing the valine precursor, acetolactate. The 2 enzymes differed in their pH optima, Km values for pyruvate and in their sensitivity to inhibition by L-valine and L-isoleucine. Both acetolactate-forming enzymes were virtually absent from the dormant pea seed, but this material did possess a 3rd pyruvate decarboxylase with the ability to form acetoin, acetaldehyde and traces of acetolactate when supplied with pyruvate at high concentrations.