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Role of Metal Cations in the Regulation of NADP-linked Isocitrate Dehydrogenase From Porcine Heart

Role of Metal Cations in the Regulation of NADP-linked Isocitrate Dehydrogenase From Porcine Heart

K Murakami, S Iwata, M Haneda, M Yoshino

Biometals. 1997 Jul;10(3):169-74.

PMID: 9243796

Abstract:

The regulatory role of divalent metal cations in the NADP-linked isocitrate dehydrogenase (EC 1.1.1.42) from porcine heart was analysed. Saturation curves with respect to the substrate threo-DS-isocitrate complexed with the metals including manganous, cadmium, cobaltous and zinc ions showed sigmoid relationships characteristic of allosteric enzymes. The Hill's interaction coefficients were 1.90, 1.75, 1.28 and 1.12, respectively. Saturation kinetics of the substrate-metal complexes including magnesium, ferrous and nickel ions exhibited normal hyperbolic curves with Hill's coefficients of 1. The ionic radii of metal cations were closely correlated with the maximal velocity, the enzyme affinity and the Hill's n11 values for the substrate-metal complexes. Cooperative interactions of metal-substrate complexes with NADP-isocitrate dehydrogenase are discussed in relation to the sites of the enzyme for the binding of the metal-substrate complex.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9028482-C	Isocitric Dehydrogenase (NADP) from porcine heart		9028-48-2	Price

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