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The role that PEPCK-C plays in gluconeogenesis may be mediated by the citric acid cycle, the activity of which was found to be directly related to PEPCK-C abundance. [15] PEPCK-C levels alone were not highly correlated with gluconeogenesis in the mouse liver, as previous studies have suggested. [15]
Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49, phosphopyruvate carboxylase (ATP), phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, phosphopyruvate carboxykinase (adenosine triphosphate), PEP carboxylase, PEP carboxykinase, PEPCK (ATP), PEPK, PEPCK, phosphoenolpyruvic carboxylase, phosphoenolpyruvic carboxykinase, phosphoenolpyruvate carboxylase (ATP), phosphopyruvate ...
Phosphoenolpyruvate carboxykinase 2, mitochondrial (PCK2, PEPCK-M), is an isozyme of phosphoenolpyruvate carboxykinase (PCK, PEPCK) that in humans is encoded by the PCK2 gene on chromosome 14. This gene encodes a mitochondrial enzyme that catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) in the presence of guanosine ...
The location of the enzyme that links these two parts of gluconeogenesis by converting oxaloacetate to PEP – PEP carboxykinase (PEPCK) – is variable by species: it can be found entirely within the mitochondria, entirely within the cytosol, or dispersed evenly between the two, as it is in humans. [27]
18534 Ensembl ENSG00000124253 ENSMUSG00000027513 UniProt P35558 Q9Z2V4 RefSeq (mRNA) NM_002591 NM_011044 RefSeq (protein) NP_002582 NP_035174 Location (UCSC) Chr 20: 57.56 – 57.57 Mb Chr 2: 172.99 – 173 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Phosphoenolpyruvate carboxykinase 1 (soluble), also known as PCK1, is an enzyme which in humans is encoded by the PCK1 gene ...
The fate of PEP is still debated. The simplest explanation is that PEP would diffuse back to the mesophyll to serve as a substrate for PEPC. Because PEPCK uses only one ATP molecule, the regeneration of PEP through PEPCK would theoretically increase photosynthetic efficiency of this subtype, however this has never been measured.
Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO 3 −) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: [1]
This reaction is catalyzed by the enzyme phosphoenolpyruvate carboxykinase (PEPCK). This reaction is a rate-limiting step in gluconeogenesis: [ 3 ] GTP + oxaloacetate → GDP + phosphoenolpyruvate + CO 2