Purification and Properties of Fumarate Reductase from Bakers Yeast

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概要

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• Fumarate reductase was highly purified from the cytosol fraction of the cells of bakers yeast, which were anaerobically cultured, with a yield of 6% by 7 steps. The purified enzyme is homogeneous in disc-gel electrophoresis, and has a molecular weight of 58, 800. Its isoelectric point is 5.3. The enzyme contains 1 molecule of non-covalently bound FAD per molecule of protein. Non-heme iron was not detected. The amino acid composition was determined. The spectra of the enzyme showed absorption peaks at 273, 380 and 456 nm with shoulders at 370, 440 and 478 nm. The fluorescence spectra showed excitation peaks at 452 and 368 nm and an emission peak at 500 nm. Double-reciprocal plots of the reaction rate against the FADH2 and FMNH2 concentrations curved upwards. The hill coefficient values and S0.5 for FADH2 and FMNH2 were estimated to be 1.6 and 0.21 μM, and 1.5 and 0.38μM, respectively. The Km for fumarate was 0.2mM.

• 社団法人 日本農芸化学会の論文

著者

• MURATSUBAKI HARUHIRO

  Section of Clinical Biochemistry, School of Health Science, Kyorin University

• Muratsubaki Haruhiro

  Section Of Clinical Biochemistry School Of Health Science Kyorin University

• KATSUME Takuro

  Section of Clinical Biochemistry, School of Health Science, Kyorin University

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• Effect of Gene Disruptions of the TCA Cycle on Production of Succinic Acid in Saccharomyces cerevisiae
• Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth
• Purification and Properties of Fumarate Reductase from Bakers Yeast

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