Ligands of the Mn2+ Bound to Porcine Mitochondrial NADP-Dependent Isocitrate Dehydrogenase, as Assessed by Mutagenesis

Pig heart mitochondrial NADP-dependent isocitrate dehydrogenase requires a divalent metal ion for catalysis, and metal-isocitrate is its preferred substrate. On the basis of the crystal structure of the enzyme−Mn2+−isocitrate complex, Asp252, Asp275, and Asp279 were selected as targets for site-dire...

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Veröffentlicht in:	Biochemistry (Easton) 2004-03, Vol.43 (10), p.2821-2828
Hauptverfasser:	Huang, Yu Chu, Grodsky, Neil B, Kim, Tae-Kang, Colman, Roberta F
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Aspartic Acid - genetics Binding Sites - genetics Cations, Divalent - chemistry Circular Dichroism Hydrogen-Ion Concentration Isocitrate Dehydrogenase - biosynthesis Isocitrate Dehydrogenase - chemistry Isocitrate Dehydrogenase - genetics Isocitrate Dehydrogenase - isolation & purification Kinetics Ligands Manganese - chemistry Mitochondria, Heart - enzymology Mitochondria, Heart - genetics Mutagenesis, Site-Directed Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Substrate Specificity - genetics Swine
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