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.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Liao CL,Atkinson DEdoi
10.1128/JB.106.1.31-36.1971subject
Has Abstractpub_date
1971-04-01 00:00:00pages
31-6issue
1eissn
0021-9193issn
1098-5530journal_volume
106pub_type
杂志文章abstract::Spores were isolated from the filamentous cyanobacterium Anabaena cylindrica, and their deoxyribonucleic acid, ribonucleic acid, and protein compositions were determined. ...
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journal_title:Journal of bacteriology
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