background:
PCK2 is a a member of the phosphoenolpyruvate carboxykinase (GTP) family. The protein is a mitochondrial enzyme that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the presence of GTP. A cytosolic form encoded by a different gene has also been characterized and is the key enzyme of gluconeogenesis in the liver. The encoded protein may serve a similar function, although it is constitutively expressed and not modulated by hormones such as glucagon and insulin that regulate the cytosolic form. Alternatively spliced transcript variants have been described.
Function:
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (By similarity).
Subunit:
Monomer.
Subcellular Location:
Mitochondrion.
Post-translational modifications:
Phosphorylated upon DNA damage, probably by ATM or ATR.
DISEASE:
Defects in PCK2 are the cause of mitochondrial phosphoenolpyruvate carboxykinase deficiency (M-PEPCKD) [MIM:261650]. A metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autoposy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait.
Similarity:
Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.
Database links:
UniProtKB/Swiss-Prot: Q16822.3
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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