OCCURRENCE AND PROPERTIES OF L-AMINOACID:2-GLYOXYLATE AMINOTRANSFERASE IN PLANTS

Abstract

Extracts prepared from a variety of higher plant tissues have been examined for L-aminoacid: 2-glyoxylate aminotransferase (glyoxylate transaminase) activity. This enzyme has been detected in extracts prepared from sunflower cotyledons, corn coleoptiles, mature pea leaves, and carrot storage tissues. Measurement of glyoxylate transaminase activity was based on ability of the extracts to convert glyoxylate-1,2,-C14 to glycine-1, 2-C14 in the presence of a suitable amino group donor. Properties of this enzyme system, including amino donor requirements, inhibition, pH optima, and reversibility, have been studied using extracts prepared from mature pea leaves. In sunflower cotyledons, glyoxylate transaminase activity decreased during germination. Studies of the intracellular localization of this enzyme have shown that glyoxylate transamination occurs mainly in the cytoplasm.