Serine: glyoxylate aminotransferase exerts no control on photosynthesis

• Published in: Journal of experimental botany Vol. 50; no. 334; pp. 719 - 722
• Main Authors: Wingler, Astrid, Ann, Victoria J., Lea, Peter J., Leegood, Richard C.
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01-05-1999; OXFORD UNIVERSITY PRESS
• Subjects: Agronomy. Soil science and plant productions; Amino acids; Barley; Biological and medical sciences; Calvin cycle; Chlorophylls; Economic plant physiology; Enzymes; Fundamental and applied biological sciences. Psychology; Glyoxylates; Leaves; Metabolism; Mutants; Net assimilation, photosynthesis, carbon metabolism. Photorespiration, respiration, fermentation (anoxia, hypoxia); Nutrition. Photosynthesis. Respiration. Metabolism; Photorespiration; Photosynthesis; Photosynthesis, respiration. Anabolism, catabolism; Plant physiology and development; Plants; serine; serine:glyoxylate aminotransferase; SHORT COMMUNICATION; Monocotyledones; Hordeum vulgare; Enzyme; Transferases; Serine; Genetic variant; Functional deficit; Serine-glyoxylate transaminase; Cereal crop; Regulation(control); Gramineae; Photorespiration; Aminoacid; Transaminases; Angiospermae; Spermatophyta; Photosynthesis
• ISSN: 0022-0957; 1460-2431
• DOI: 10.1093/jxb/50.334.719

A barley (Hordeum vulgare L.) mutant deficient in serine:glyoxylate aminotransferase (SGAT) was crossed with wild-type plants to generate heterozygous mutants. Plants of the F2 generation with reduced SGAT activities (45–60% of wild-type activities) contained proportionally less SGAT protein. Reduced SGAT activities resulted in the accumulation of serine and, to a smaller extent, of glycine, indicating that the flux through the photorespiratory pathway was restricted. Rates of photosynthesis were, however, not affected by the reduction in SGAT activity.