Regulatory characteristics of phosphoenolpyruvate carboxylase from the extreme thermophile, Thermus aquaticus.
Phosphoenolpyruvate carboxylase from the extremely thermophilic bacterium, Thermus aquaticus YT-1, exhibits a virtually absolute requirement for acetyl CoA and there is strong positive cooperativity in the interaction of this activator with the enzyme. Several tricarboxylic acid cycle intermediates inhibit the enzyme. These findings suggest an anaplerotic role for the enzyme and an allosteric modulation of its activity by acetyl CoA and tricarboxylic acid cycle intermediates.
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000494:Allosteric Regulation; D002262:Carboxy-Lyases / Q000378:metabolism*; D007700:Kinetics; D010730:Phosphoenolpyruvate Carboxylase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013824:Thermus / Q000201:enzymology*
D000105:Acetyl Coenzyme A; D002262:Carboxy-Lyases; D010730:Phosphoenolpyruvate Carboxylase