The assembly mechanism of the lactate dehydrogenase tetramer from Bacillus stearothermophilus; the equilibrium relationships between quaternary structure and the binding of fructose 1,6-biphosphate, NADH and oxamate-Reference-Cited by-同舟云学术

The assembly mechanism of the lactate dehydrogenase tetramer from Bacillus stearothermophilus; the equilibrium relationships between quaternary structure and the binding of fructose 1,6-biphosphate, NADH and oxamate

Published:1985-07 Issue:3 Volume:829 Page:387-396
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Clarke Anthony R.,Atkinson Tony,Campbell John W.,John Holbrook J.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference23 articles.

1. Structure and Function of L-Lactate Dehydrogenases from Thermophilic and Mesophilic Bacteria. I) Isolation and Characterization of Lactate Dehydrogenases from Thermophilic and Mesophilic Bacilli

2. Comparative studies of lactic acid dehydrogenases in lactic acid bacteria

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

4. Fructose-1,6-diphosphate Requirement of Streptococcal Lactic Dehydrogenases

5. Fructose 1,6-diphosphate-activated L-lactate dehydrogenase from Streptococcus lactis: kinetic properties and factors affecting activation

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