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PMID: 5551640 Published · ppublish English Journal Article

Regulation at the phosphoenolpyruvate branchpoint in Azotobacter vinelandii: phosphoenolpyruvate carboxylase.

Journal of bacteriology ·Vol. 106 ·No. 1 ·1971-04-00 ·Pages 31-6

Liao CL, Atkinson DE

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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22 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1971-04-00
Pages
31-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC248640
Subset
IM
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