By Dennis E. Buetow (Eds.)
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Extra resources for Subcellular Biochemistry and Molecular Biology
Gracilis Z and var. bacillaris, NADH-coenzyme Q reductase activity, which was rotenone sensitive, was coupled to site I of the electron-transfer system (Sharpless and Butow, 1970a). The mitochondrial preparation also showed a ferricyanide reduction activity with succinate in the presence of rotenone and cyanide. This activity was markedly inhibited by antimycin A, and the phosphorylation, with a low P/O ratio and coupled to the ferricyanide reduction, was also severely inhibited. These results suggested the presence of site II with participation of cytochrome b, disproving the early suggestion of Buetow and Buchanan (1965).
193 mM, depending on the concentration of the diphosphate. This enzyme was inhibited by potassium fluoride, phosphate, and Ca2 + ; ATP, ADP, and UDP-glucose were not inhibitory. Euglena α-phosphoglucomutase acts on α-glucose l-phosphate that is produced from paramylon by the action of laminaribiose phosphorylase and β-1,3oligoglucan phosphorylase, while the ß-mutase acts on ß-glucose 1-phosphate produced from trehalose by trehalose phosphorylase. Both reactions yield glucose 6-phosphate, which is then metabolized by the glycolytic pathway.
Inui et al. (1982, 1984b) found another type of pyruvate dehydrogenase that employed NADP, methylviologen, or FAD as the electron acceptor. This enzyme was strongly inhibited by oxygen and its properties resembled those of pyruvate synthase present in anaerobic bacteria. It considered to be the key regulating enzyme in wax ester fermentation, the energy-generating system in Euglena under anaerobic conditions (see Section VI,A). Citrate synthase activity was detected in both the particulate and the soluble fractions from a bleached mutant (SM-L1) of E.
Subcellular Biochemistry and Molecular Biology by Dennis E. Buetow (Eds.)
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