Heat-Stable and Fructose 1,6-Bisphosphate-Activated L-Lactate Dehydrogenase from an Extremely Thermophilic Bacterium1
- 1 April 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 91 (4), 1343-1348
- https://doi.org/10.1093/oxfordjournals.jbchem.a133821
Abstract
Heat-stable L-lactate dehydrogenase [EC 1.1.1.27] 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.Keywords
This publication has 1 reference indexed in Scilit:
- Glucose Fermentation Pathway of Thermoanaerobium brockiiJournal of Bacteriology, 1980