Arg-94 is crucial to the catalysis of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8
Author:
Publisher
Elsevier BV
Subject
Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis
Reference22 articles.
1. Cloning of 3-Isopropylmalate Dehydrogenase Gene of an Extreme Thermophile and Partial Purification of the Gene Product
2. High guanine plus cytosine content in the third letter of codons of an extreme thermophile. DNA sequence of the isopropylmalate dehydrogenase of Thermus thermophilus.
3. Purification, Catalytic Properties, and Thermal Stability of Threo-Ds-3-Isopropylmalate Dehydrogenase Coded by leuB Gene from an Extreme Thermophile, Thermus thermophilus Strain HB81
4. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
5. Structure of 3–isopropylmalate dehydrogenase in complex with NAD+: ligand–induced loop closing and mechanism for cofactor specificity
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure;Biochemistry;2016-01-14
2. Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis;FEBS Journal;2014-10-04
3. Piezo-Adapted 3-Isopropylmalate Dehydrogenase of the Obligate PiezophileShewanella benthicaDB21MT-2 Isolated from the 11,000-m Depth of the Mariana Trench;Bioscience, Biotechnology, and Biochemistry;2009-11-23
4. Novel Substrate Specificity of Designer 3-Isopropylmalate Dehydrogenase Derived from Thermus thermophilus HB8;Bioscience, Biotechnology, and Biochemistry;2001-01
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