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In cell biology, protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family.
In the Arrhenius model of reaction rates, activation energy is the minimum amount of energy that must be available to reactants for a chemical reaction to occur. [1] The activation energy ( E a ) of a reaction is measured in kilojoules per mole (kJ/mol) or kilocalories per mole (kcal/mol). [ 2 ]
18750 Ensembl ENSG00000154229 ENSMUSG00000050965 UniProt P17252 P20444 RefSeq (mRNA) NM_002737 NM_011101 RefSeq (protein) NP_002728 NP_035231 Location (UCSC) Chr 17: 66.3 – 66.81 Mb Chr 11: 107.82 – 108.23 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein kinase C alpha (PKCα) is an enzyme that in humans is encoded by the PRKCA gene. Function Protein kinase C (PKC) is a ...
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by the second messenger diacylglycerol. [6] PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways.
Human PRKCE gene (Ensembl ID: ENSG00000171132) encodes the protein PKCε (Uniprot ID: Q02156), which is 737 amino acids in length with a molecular weight of 83.7 kDa. The PKC family of serine-threonine kinases contains thirteen PKC isoforms, and each isoform can be distinguished by differences in primary structure, gene expression, subcellular localization, and modes of activation. [7]
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. [2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants. [3]
Glutathione peroxidase 3 (GPx-3), also known as plasma glutathione peroxidase (GPx-P) or extracellular glutathione peroxidase is an enzyme that in humans is encoded by the GPX3 gene. [5] [6] [7] GPx-3 belongs to the glutathione peroxidase family, which functions in the detoxification of
PKC-zeta has an N-terminal regulatory domain, followed by a hinge region and a C-terminal catalytic domain. Second messengers stimulate PKCs by binding to the regulatory domain, translocating the enzyme from cytosol to membrane, and producing a conformational change that removes auto-inhibition of the PKC catalytic protein kinase activity.