Ligands of the Mn2+ Bound to Porcine Mitochondrial NADP-Dependent Isocitrate Dehydrogenase, as Assessed by Mutagenesis
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19176
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi030253f
Reference35 articles.
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1. Liposomes modified with cardiolipin can act as a platform to regulate the potential flux of NADP + -dependent isocitrate dehydrogenase;Metabolic Engineering Communications;2016-12
2. Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure;Biochemistry;2016-01-14
3. Unveiling the Catalytic Mechanism of NADP+-Dependent Isocitrate Dehydrogenase with QM/MM Calculations;ACS Catalysis;2015-12-15
4. Transient kinetic studies reveal isomerization steps along the kinetic pathway ofThermus thermophilus3-isopropylmalate dehydrogenase;FEBS Journal;2013-03-11
5. Induced Fit and the Catalytic Mechanism of Isocitrate Dehydrogenase;Biochemistry;2012-08-27
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