Pyruvate:NADP+ oxidoreductase is stabilized by its cofactor, thiamin pyrophosphate, in mitochondria of Euglena gracilis
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. The origin of pyruvate:NADP+ oxidoreductase in mitochondria of Euglena gracilis
2. Occurrence of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in mitochondria of Euglena gracilis
3. Purification and characterization of pyruvate:NADP+ oxidoreductase in Euglena gracilis.
4. Pyruvate:NADP+ oxidoreductase from Euglena gracilis: Limited proteolysis of the enzyme with trypsin
5. Pyruvate:NADP+ oxidoreductase from Euglena gracilis: Mechanism of O2-inactivation of the enzyme and its stability in the aerobe
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1. Induction of photosynthesis under anoxic condition in Thalassiosira pseudonana and Euglena gracilis: interactions between fermentation and photosynthesis;Frontiers in Plant Science;2023-07-25
2. Energy metabolism in anaerobic eukaryotes and Earth's late oxygenation;Free Radical Biology and Medicine;2019-08
3. Physiological functions of pyruvate:NADP+ oxidoreductase and 2-oxoglutarate decarboxylase in Euglena gracilis under aerobic and anaerobic conditions;Bioscience, Biotechnology, and Biochemistry;2017-07-03
4. Biochemistry and Physiology of Vitamins in Euglena;Advances in Experimental Medicine and Biology;2017
5. The Mitochondrion of Euglena gracilis;Advances in Experimental Medicine and Biology;2017
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