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Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium.

Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Research Abstract Details 

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  • Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. Abstract Text:

    h taguchiH Taguchi,m yamashitaM Yamashita,h matsuzawaH Matsuzawa,t ohtaT Ohta,

    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

    h taguchiH Taguchi,m yamashitaM Yamashita,h matsuzawaH Matsuzawa,t ohtaT Ohta,

    For similar bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus research abstracts see: bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus research

    PUBMED ID PMID:

    MEDLINE DATE:

    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

    Grant and Affiliation Information for Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium.

    AFFILIATION:

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    ACRONYM:

    MEDLINETA: J Biochem

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    Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium Related Publications

     

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