Metabolism and decarboxylation of glycollate and serine in leaf peroxisomes

• Published in: Planta 1981-11, Vol.153 (3), p.225-231
• Main Authors: Walton, N.J, Butt, V.S
• Format: Article
• Language: English
• Subjects: Decarboxylation; Dehydrogenases; Glyoxylates; Leaves; Oxidases; Oxidation; Peroxisomes; plant biochemistry; plant physiology; Plants; Spinach; Ungulates
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/BF00383891

The linked utilization of glycollate and L-serine has been studied in peroxisomal preparations from leaves of spinach beet (Beta vulgaris L.). The generation of glycine from glycollate was found to be balanced by the production of hydroxypyruvate from serine and similarly by 2-oxoglutarate when L-glutamate was substituted for L-serine. In the presence of L-malate and catalytic quantities of NAD+, about 40% of the hydroxypyruvate was converted further to glycerate, whereas with substrate quantities of NADH, this conversion was almost quantitative. CO2 was released from the carboxyl groups of both glycollate and serine. Since the decarboxylation of both substrates was greatly increased by the catalase inhibitor, 3-amino-1,2,4-triazole, and abolished by bovine liver catalase, it was attributed to the non-enzymic attack of H2O2, generated in glycollate oxidation, upon glyoxylate and hydroxypyruvate respectively. At 25—30° C, about 10% of the glyoxylate and hydroxypyruvate accumulated was decarboxylated, and the release of CO2 from each keto-acid was related to the amounts present. It is suggested that hydroxypyruvate decarboxylation might contribute significantly to photorespiration and provide a metabolic route for the complete oxidation of glycollate, the magnitude of this contribution depending upon the concentrations of glyoxylate and hydroxypyruvate in the peroxisomes.