phosphoenolpyruvate carboxylase

(redirected from PEP carboxylase)

phosphoenolpyruvate carboxylase

An enzyme that catalyses a two-step reaction: formation of carboxyphosphate and enolate form of pyruvate, and carboxylation of enolate with the release of phosphate. It replenishes oxaloacetate in the tricarboxylic acid cycle when operating in reverse. Phosphoenolpyruvate carboxylase is the recommended name for EC 4.1.1.31, orthophosphate:oxaloacetate carboxy-lyase (phosphorylating).

Phosphoenolpyruvate carboxylase  has also been used for:
(1) Phosphoenolpyruvate carboxykinase (GTP), EC 4.1.1.32 (GTP:oxaloacetate carboxy-lyase (transphosphorylating));
(2) Phosphoenolpyruvate carboxykinase (pyrophosphate), EC 4.1.1.38 (pyrophosphate:oxaloacetate carboxy-lyase (transphosphorylating)); and
(3) Phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49 (ATP:oxaloacetate carboxy-lyase (transphosphorylating)).
References in periodicals archive ?
PEP carboxylase has been the subject of extensive experimental research in the last decades [1,2].
Physical and kinetic properties of photosynthetic PEP carboxylase in developing apple fruit.
However, recent studies ensure that the activity of pyruvate carboxylase is prominent over PEP carboxylase (PetersWendisch, et al.
PEP carboxylase and malic enzyme play a vital role for channeling pyruvate pool, while C.
It should be noted that both PEP carboxylase and PYR carboxylase were active when the organism operated through mode 47 and only PYR carboxylase was active when the organism operated through mode 48.
Here, the activity of the PEP carboxylase (25) was half of the PYR carboxylase, while the activity of malic enzyme was zero.
Further, the activities of both PYR carboxylase and PEP carboxylase were less than as compared to maximum lysine synthesis case.