Some properties of NAD-independent α-glycerophosphate dehydrogenase of yeast

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概要

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• NAD-independent, mitochondrial α-glycerophosphate dehydrogenase of baker's yeast, Saccharomyces cerevisiae, was liberated from cells and its nature was examined. Hydrogen acceptors, pH optima and reaction rates with substrate and hydrogen acceptor of the enzyme were determined. A naturally occurring phenolic pigment extracted from yeast cells was also found to function as an effective hydrogen acceptor for the enzyme. Addition of FMN or FAD to the α-glycerophosphate oxidation system largely accelerated enzymatic activity, whereas the enzyme system was strongly blocked by SH-reagents. This suggests that the SH-group functions at an essential site. Clear-cut inhibition by antimycin A of electron transfer to cytochrome c suggests the intermediation of cytochrome b.

• 日本植物生理学会の論文

著者

• NAGAHISA MASASHI

  Biological Laboratory, Tokyo Institute of Technology

• Nagahisa Masashi

  Biological Laboratory Tokyo Institute Of Technology

• MIYATA KEIJIRO

  Biological Laboratory, Tokyo Institute of Technology

• Miyata Keijiro

  Biological Laboratory Tokyo Institute Of Technology

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• A phenolic pigment as a hydrogen carrier in D-lactate cytochrome c reductase system of a yeast
• Some properties of NAD-independent α-glycerophosphate dehydrogenase of yeast
• Development of catalase activity in yeast in relation to growth and respiration

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