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. 1974 Jan;137(1):45–53. doi: 10.1042/bj1370045

Regulation of `malic' enzyme of Solanum tuberosum by metabolites

D D Davies 1, K D Patil 1
PMCID: PMC1166078  PMID: 4150731

Abstract

A purification of `malic' enzyme from potato is described. The purified enzyme is specific for NADP and requires a bivalent cation for activity. At pH values below 7 the plot of rate versus malate concentration approximates to normal Michaelis–Menten kinetics. At pH values above 7 the plot of rate versus malate concentration is sigmoid. A number of dicarboxylic acids activate the enzyme and remove the sigmoidicity. The enzyme is inhibited by phosphate, triose phosphates and AMP. In general, effectors of the oxidative decarboxylation of malate behave in the same manner in the reductive carboxylation of pyruvate. The response of the enzyme to energy charge is reported and the physiological significance of the response to metabolites is discussed in relation to the proposed role of the enzyme in the control of pH.

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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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