A Glutamyl Residue in the Active Site of Triphosphopyridine Nucleotide-dependent Isocitrate Dehydrogenase of Pig Heart
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Evidence for a methionyl residue in the active site of isocitrate dehydrogenase
2. Effect of Modification of a Methionyl Residue on the Kinetic and Molecular Properties of Isocitrate Dehydrogenase
3. Role of sulfhydryl groups in the catalytic function of isocitrate dehydrogenase. I. Reaction with 5,5'-dithiobis(2-nitrobenzoic acid)
4. The Role of Sulfhydryl Groups in the Catalytic Function of Isocitrate Dehydrogenase
5. The Role of Sulfhydryl Groups in the Catalytic Function of Isocitrate Dehydrogenase
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1. Possible Role of Carboxyl and Imidazole Groups in the Catalysis of Pummelo Limonoid Glucosyltransferase;Chinese Journal of Catalysis;2010-01
2. Critical Role of Lys212 and Tyr140 in Porcine NADP-dependent Isocitrate Dehydrogenase;Journal of Biological Chemistry;2003-12
3. Crystal Structure of Porcine Mitochondrial NADP+-dependent Isocitrate Dehydrogenase Complexed with Mn2+ and Isocitrate;Journal of Biological Chemistry;2002-11
4. Evaluation by Mutagenesis of the Roles of His309, His315, and His319 in the Coenzyme Site of Pig Heart NADP-Dependent Isocitrate Dehydrogenase;Biochemistry;2002-04-01
5. Evaluation by Site-Directed Mutagenesis of Aspartic Acid Residues in the Metal Site of Pig Heart NADP-Dependent Isocitrate Dehydrogenase;Biochemistry;2000-02-08
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