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. 1982 Oct;70(4):1169–1172. doi: 10.1104/pp.70.4.1169

Kinetic Ramifications of the Association-Dissociation Behavior of NAD Malic Enzyme 1

A Possible Regulatory Mechanism

Scott D Grover 1, Randolph T Wedding 1
PMCID: PMC1065845  PMID: 16662633

Abstract

NAD malic enzyme can exist in dimer, tetramer, or octamer form. Freshly prepared enzyme from Solanum tuberosum var. Chieftan exists predominantly as the octamer and during storage is progressively converted into lower molecular weight forms. High ionic strength favors dimer formation, whereas high concentrations of malate or citrate favor tetramer formation. The tetramer is the most active form, having a low Km for malate and a high Vmax. The dimer, with its high Km and low Vmax, is the least active form. Malate may regulate NAD malic enzyme by controlling its state of oligomerization.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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