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J Bacteriol. 1971 April; 106(1): 31-36
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Regulation at the Phosphoenolpyruvate Branchpoint in Azotobacter vinelandii: Phosphoenolpyruvate Carboxylase

^a Biochemistry Division, Department of Chemistry, University of California, Los Angeles, California 90024

ABSTRACT

Phosphoenolpyruvate carboxylase (EC 4.1.1.31) from Azotobacter vinelandii, like the corresponding enzyme from other organisms, is activated by acetyl coenzyme A and inhibited by L-aspartate. Both modifiers affect primarily the affinity of the enzyme for phosphoenolpyruvate. This is the first enzyme with a strictly anaplerotic (intermediate-replacing) function to be tested for response to the adenylate energy charge; it is entirely insensitive to variation in charge. The results suggest that carboxylation of phosphoenolpyruvate in this organism is controlled by negative feedback from aspartate and by the stimulatory effect of acetyl coenzyme A. The adenylate energy charge may be expected to affect the rate of this reaction indirectly through its effects on the concentrations of acetyl coenzyme A and L-aspartate.

¹ Present address: Department of Biochemistry, University of California, Berkeley, Calif. 94720.

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