Engineering 6-phosphogluconate dehydrogenase improves grain yield in heat-stressed maize
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چکیده
منابع مشابه
Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate
Two crystal structures of recombinant Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase (Gs6PDH) in complex with the substrate 6-phosphogluconate have been determined at medium resolution. Gs6PDH shares significant sequence identity and structural similarity with the enzymes from Lactococcus lactis, sheep liver and the protozoan parasite Trypanosoma brucei, for which a range of st...
متن کاملImproving ethanol yield in acetate-reducing Saccharomyces cerevisiae by cofactor engineering of 6-phosphogluconate dehydrogenase and deletion of ALD6
BACKGROUND Acetic acid, an inhibitor of sugar fermentation by yeast, is invariably present in lignocellulosic hydrolysates which are used or considered as feedstocks for yeast-based bioethanol production. Saccharomyces cerevisiae strains have been constructed, in which anaerobic reduction of acetic acid to ethanol replaces glycerol formation as a mechanism for reoxidizing NADH formed in biosynt...
متن کامل6-Phosphogluconate dehydrogenase from leuconostoc mesenteroides.
The pathways for degradation of 6-phosphogluconate have been rather clearly defined for several organisms, the most notable of which are yeast (Horecker, 1953), Escherichia coli (Cohen, 1951), Pseudomonas saccharophila (Entner and Doudoroff, 1952; MacGee and Doudoroff, 1954), and Pseudomonas fluorescens (Kovachevich and Wood, 1954). The enzymes from yeast and E. coli appear to be similar, if no...
متن کاملDietary regulation of 6-phosphogluconate dehydrogenase synthesis.
The relative rates of synthesis and degradation for rat liver 6-phosphogluconate dehydrogenase have been determined in animals maintained at several dietary states. Relative rates of synthesis were determined by pulse-labeling the enzyme either in live rats and determining the radioactivity in the purified enzyme or in whole cell suspensions of hepatocytes followed by precipitation of the enzym...
متن کاملPurification and characterization of cytosolic 6-phosphogluconate dehydrogenase isozymes from maize.
Cytosolic isozymes of 6-phosphogluconate dehydrogenase were purified from roots of maize (Zea mays L.). The final preparation contained two 55-kD proteins. Affinity-purified dehydrogenases from a maize line that is null for both cytosolic 6-phosphogluconate dehydrogenase isozymes (Pgd1-null, Pgd2-null) lacked the 55-kD proteins. The substrate kinetics of the purified enzyme were determined.
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2020
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.2010179117