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. 1974 Jun;53(6):829–834. doi: 10.1104/pp.53.6.829

Phosphoenolpyruvate Carboxylase from Spinach Leaf Tissue

Inhibition by Sulfite Ion 1

S K Mukerji a,2, S F Yang a
PMCID: PMC541457  PMID: 16658799

Abstract

Phosphoenolpyruvate carboxylase (EC 4.1.1.31), partially purified from spinach (Spinacia oleracea) leaves, is inhibited by SO32− ion. The inhibition is competitive or mixed type with respect to HCO3− (Ki = 17 mm), and noncompetitive with respect to phosphoenolpyruvic acid (Ki = 11 mm), Mg2+ (Ki = 10 mm), and Mn2+ (Ki = 2.4 mm). The inhibitory effect of SO32− is more significant in the presence of Mn2+ than in the presence of Mg2+. l-Malate, an inhibitor of phosphoenolpyruvate carboxylase activity, and SO32− may bind at the same site on the enzyme. Glyoxal bisulfite and glyoxylate bisulfite are equally effective inhibitors of the enzyme activity as SO32−, but α-hydroxypyridinemethanesulfonate is a weak inhibitor. The data are discussed in relation to the physiological effect of the air pollutant (SO2) on plant leaf metabolism.

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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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