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J. Biochem, 1982, Vol. 91, No. 4 1343-1348
© 1982 Japanese Biochemical Society

research-article

Heat-Stable and Fructose 1,6-Bisphosphate-Activated L-Lactate Dehydrogenase from an Extremely Thermophilic Bacterium1

Hayao TAGUCHI, Minoru YAMASHITA, Hiroshi MATSUZAWA and Takahisa OHTA

Department of Agricultural Chemistry, The University of Tokyo Yayoi, Bunkyo-ku, Tokyo 113

Heat-stable L-lactate dehydrogenase [EC 1.1.1.27 [EC] ] was purified from an extremely thermophilic bacterium belonging to the genus Thermus, and it showed an allosteric nature dependent on fructose 1,6-bisphosphate as an effector. The enzyme had a molecular weight of approximately 120,000 with a subunit molecular weight of 31,000. For pyruvate reduction, the optimal pH was found to be 4.5. At neutral pH, which is a more physiological region, little enzyme activity was observed, but marked reaction resulted from the addition of fructose 1,6-bisphosphate. This addition stabilized the enzyme toward heat treatment at up to 95°C. The optimal temperature for the enzyme reaction was approximately 80°C for pyruvate reduction and 95°C for lactate oxidation.

1This work was supported in part by grants from the Ministry of Education, Science and Culture of Japan.


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