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 degrees C. The optimal temperature for the enzyme reaction was approximately 80 degrees C for pyruvate reduction and 95 degrees C for lactate oxidation.
Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Publishing Authors By Initials
Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of biochemistry
VOLUME: 91
Page Numbers: 1343-8
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Apr
YEAR: 1982
Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Keywords Mesh Terms:
KEYWORDS: Thermus
MESH TERMS: enzymology
Chemical & Substance for Abstract: Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Information
Substance Name: L-Lactate Dehydrogenase
Registry Number: EC 1.1.1.27
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Country: JAPAN
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MEDLINETA: J Biochem
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