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Serine:glyoxylate aminotransferase mutant of barley

Conference · · Plant Physiol., Suppl.; (United States)
OSTI ID:6071263
A photorespiratory mutant of barley (LaPr 85/84), deficient in both of the major peaks of serine:glyoxylate aminotransferase activity detected in the wild type, also lacks serine:pyruvate and asparagine:glyoxylate aminotransferase activities. Genetic analysis of the mutation demonstrated that these three activities are all carried on the same enzyme. The mutant, when placed in air, accumulated a large pool of serine, showed the expected rate (50%) of ammonia release during photorespiration but produced CO/sub 2/ at twice the wild type rate when it was fed (/sup 14/C) glyoxylate. Compared with the wild type, LaPr 85/84 exhibited abnormal transient changes in chlorophyll a fluorescence when the CO/sub 2/ concentration of the air was altered, indicating that the rates of the fluorescence quenching mechanisms were affected in vivo by the lack of this enzyme.
Research Organization:
Univ. of Lancaster, England
OSTI ID:
6071263
Report Number(s):
CONF-8707108-
Conference Information:
Journal Name: Plant Physiol., Suppl.; (United States) Journal Volume: 83:4
Country of Publication:
United States
Language:
English