Structure and Function of L-Lactate Dehydrogenases from Thermophilic and Mesophilic Bacteria, X. Analysis of Structural Elements Responsible for the Differences in Thermostability and Activation by Fructose 1,6-bisphosphate in the Lactate. Dehydrogenases fromB. stearothermophilusandB. caldolyticusby Protein Engineering
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm3.1990.371.2.655/pdf
Reference11 articles.
1. The molecular pathway by which fructose 1,6-bisphosphate induces the assembly of a bacterial lactate dehydrogenase
2. Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus
3. 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
4. A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure
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