X-ray structures of PEPCK provide insight into the structure and the mechanism of PEPCK enzymatic activity. The mitochondrial isoform of chicken liver PEPCK complexed with Mn 2+ , Mn 2+ - phosphoenolpyruvate (PEP), and Mn 2+ -GDP provides information about its structure and how this enzyme catalyzes reactions. [ 10 ]

磷酸烯醇式丙酮酸碳羧化酶（英语：Phosphoenolpyruvate carboxykinase，或称为烯醇丙氨酸磷酸羧激酶或磷酸烯醇丙酮酸羧激酶，简称为PEPCK，EC 4.1.1.32）是以一条单一肽链构成，相对分子质量为740千道尔顿的一种激酶。

磷酸烯醇丙酮酸羧化激酶 [1] （英語： Phosphoenolpyruvate carboxykinase ，或称为烯醇丙氨酸磷酸羧激酶或磷酸烯醇丙酮酸羧激酶，简称为PEPCK，EC 4.1.1.32）是以一条单一肽链构成，相对分子质量为740千道尔顿的一种激酶。

PEPCK is the rate-limiting enzyme of gluconeogenesis in the liver and kidney, and is also a key regulator of TCA cycle flux. PEPCK can catalyze oxaloacetate into phosphoenolpyruvate (PEP) and carbon dioxide. PEPCK has two isoforms: PEPCK1 (PEPCK-C) and PEPCK2 (PEPCK-M).

磷酸烯醇丙酮酸羧化激酶 [1] （英語： Phosphoenolpyruvate carboxykinase ，或稱為烯醇丙氨酸磷酸羧激酶或磷酸烯醇丙酮酸羧激酶，簡稱為PEPCK，EC 4.1.1.32）是以一條單一肽鏈構成，相對分子質量為740千道爾頓的一種激酶。

phosphoenolpyruvate carboxykinase;PEPCK 定 义 编号：EC 4.1.1.32。在糖异生途径中，催化草酰乙酸形成磷酸烯醇式丙酮酸和二氧化碳的酶。此反应是需要鸟苷三磷酸提供磷酰基的可逆反应。该酶在三羧酸循环中催化逆反应，以回补草酰乙酸。 应用学科

2015年9月18日 · Phosphoenolpyruvate carboxykinase (PEPCK) catalyzes a committed and rate-limiting step in hepatic gluconeogenesis, and its activity is tightly regulated to maintain normal blood glucose levels. PEPCK activity is primarily modulated through hormonal control of transcription [1–3].

PEPCK exhibits several interesting features such as a) organelle-specific isoforms (cytosolic and a mitochondrial) in vertebrate clade, b) tissue-specific expression of isoforms and c) organism-specific requirement of ATP or GTP as a cofactor.

The enzyme phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) (PEPCK) 2 has the unusual distinction of being very well studied but metabolically misunderstood. As we will document in this minireview, the enzyme has been almost exclusively linked to gluconeogenesis to the point that changes in the levels of PEPCK mRNA or its activity are ...

Regarding reaction reversibility, PEPCK is responsible for regeneration of the high-energy phosphoryl donor PEP from the unstable, activated β-keto acid OAA. When coupled with pyruvate carboxylase, PEPCK reverses the essentially irreversible formation of pyruvate and ATP from PEP and ADP in the glycolytic reaction catalyzed by pyruvate kinase.