The Effects of PH and Citrate on the Activity of NicotinamideA-denine Dinucleotide-specific Isocitrate Dehydrogenase from Pea Mitochondria

Overview

Journal Biochem J

Specialty Biochemistry

Date 1969 Aug 1

PMID 4309595

Citations 7

Authors

G F Cox

D D Davies

Affiliations

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Abstract

1. The effect of pH on the co-operative activation of the NAD-specific isocitrate dehydrogenase from pea mitochondria by isocitrate is shown. 2. The interlinked effects of pH on the affinity of the NAD-specific isocitrate dehydrogenase for isocitrate and the dependence of the pH optimum on the substrate concentration are presented. 3. A consideration of the conditions of pH and substrate concentration under which citrate activates the NAD-specific isocitrate dehydrogenase demonstrates similarities between the binding of isocitrate and citrate. 4. A comparison of the effects of citrate and pH on the gross structure of the enzyme is investigated by density-gradient centrifugation. 5. The kinetic interpretations of these results are briefly considered. 6. The metabolic significance of these studies is discussed.

Citing Articles

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NAD-Linked Isocitrate Dehydrogenase: Isolation, Purification, and Characterization of the Protein from Pea Mitochondria.

McIntosh C, Oliver D Plant Physiol. 1992; 100(1):69-75.

PMID: 16653002 PMC: 1075518. DOI: 10.1104/pp.100.1.69.

NAD malic enzyme and the control of carbohydrate metabolism in potato tubers.

Jenner H, Winning B, Millar A, Tomlinson K, Leaver C, Hill S Plant Physiol. 2001; 126(3):1139-49.

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Purification and characterization of NAD-isocitrate dehydrogenase from chlamydomonas reinhardtii .

Vega Plant Physiol. 1998; 118(1):249-55.

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Nicotinamide adenine dinucleotide phosphate-specific isocitrate dehydrogenase from a higher plant. Isolation and charactertization.

Omran R, Dennis D Plant Physiol. 1971; 47(1):43-7.

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