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.
MeSH Terms
Aspartic Acid/pharmacology
Azotobacter/enzymology,growth & development,metabolism
Carboxy-Lyases/antagonists & inhibitors,isolation & purification,metabolism
Cellulose
Chemical Precipitation
Coenzyme A/pharmacology
Culture Media
Enzyme Activation
Hydrogen-Ion Concentration
Magnesium/pharmacology
Phosphoric Acids/metabolism
Pyruvate Kinase/isolation & purification,metabolism
Pyruvates/metabolism
Quaternary Ammonium Compounds
Stereoisomerism
Sulfates
Chemicals
Culture Media
Phosphoric Acids
Pyruvates
Quaternary Ammonium Compounds
Sulfates
Aspartic Acid
Cellulose
Pyruvate Kinase
Carboxy-Lyases
Magnesium
Coenzyme A
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Liao C L
Atkinson D E
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