A mutant of barley lacking NADH-hydroxypyruvate reductase
- Univ. of Lancaster (England)
A mutant of barley, LaPr 88/29, deficient in peroxisomal NADH-hydroxypyruvate reductase (HPR) activity has been identified. Compared to the wild type the activities of NADH-HPR and NADPH-HPR were severely reduced but the mutant was still capable of fixing CO{sub 2} at rates equivalent to 75% of that of the wild type in air. Although lacking an enzyme in the main photorespiratory pathway, there appeared to be little disruption to photorespiratory metabolism as ammonia release, CO{sub 2} efflux and {sup 14}CO{sub 2} release from L-(U-{sup 14}C) serine were similar in both mutant and wild type. LaPr 88/29 has been used to show that NADH-glyoxylate reductase (GR) and NADH-HPR are probably not catalyzed by the same enzyme in barley and that over 80% of the NADPH-HPR activity is due to the NADH-HPR enzyme. Immunological studies, using antibodies raised against spinach HPR, have shown that the NADH-dependent enzyme protein is absent in LaPr 88/29 but there appears to be enhanced synthesis of the NADPH-dependent enzyme protein.
- OSTI ID:
- 6650266
- Journal Information:
- Plant Physiology, Supplement; (USA), Vol. 89:4; ISSN 0079-2241
- Country of Publication:
- United States
- Language:
- English
Similar Records
Further studies on O sub 2 -resistant photosynthesis and photorespiration in a tobacco mutant with enhanced catalase activity
Serine:glyoxylate aminotransferase mutant of barley
Related Subjects
BARLEY
CARBON DIOXIDE FIXATION
OXIDOREDUCTASES
ENZYME ACTIVITY
BIOLOGICAL PATHWAYS
CARBON 14 COMPOUNDS
CARBON DIOXIDE
MUTANTS
NADH2
PHOTOSYNTHESIS
SERINE
TRACER TECHNIQUES
AMINO ACIDS
CARBON COMPOUNDS
CARBON OXIDES
CARBOXYLIC ACIDS
CEREALS
CHALCOGENIDES
CHEMICAL REACTIONS
COENZYMES
ENZYMES
GRASS
HYDROXY ACIDS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
LILIOPSIDA
MAGNOLIOPHYTA
NUCLEOTIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXIDES
OXYGEN COMPOUNDS
PHOTOCHEMICAL REACTIONS
PLANTS
SYNTHESIS
550201* - Biochemistry- Tracer Techniques