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A thermostable fumarase was purified from a strain ofThermus thermophilusisolated from a Japanese hot spring. The maximum specific activity of the purified enzyme was 1740 units/mg at pH 8.0 and 85°C. The enzyme was composed of four identical subunits with a molecular weight of 46,000 and displayed other enzymatic characteristics which are common to the class II fumarases. The thermal stability of...
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