Characterization of Homoisocitrate Dehydrogenase Involved in Lysine Biosynthesis of an Extremely Thermophilic Bacterium,Thermus thermophilus HB27, and Evolutionary Implication of β-Decarboxylating Dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference42 articles.
1. ENZYME RECRUITMENT IN EVOLUTION OF NEW FUNCTION
2. Molecular and phylogenetic characterization of isopropylmalate dehydrogenase of a thermoacidophilic archaeon, Sulfolobus sp. strain 7
3. Functional prediction: Identification of protein orthologs and paralogs
4. Comparison of Isocitrate Dehydrogenase from Three Hyperthermophiles Reveals Differences in Thermostability, Cofactor Specificity, Oligomeric State, and Phylogenetic Affiliation
5. Conversion of the Coenzyme Specificity of Isocitrate Dehydrogenase by Module Replacement
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1. Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily;Communications Biology;2021-06-07
2. Promiscuous activity of 3‐isopropylmalate dehydrogenase produced at physiological level affords Escherichia coli growth on d ‐malate;FEBS Letters;2020-06-02
3. Structure, function, and regulation of enzymes involved in amino acid metabolism of bacteria and archaea;Bioscience, Biotechnology, and Biochemistry;2017-11-02
4. Structure and function of an ancestral-type β-decarboxylating dehydrogenase from Thermococcus kodakarensis;Biochemical Journal;2016-12-22
5. Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius;Extremophiles;2016-09-02
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