Recombinant Human GCAT protein (denatured) is a Human Full Length protein, in the 22 to 419 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA.
KBL, GCAT, AKB ligase, Aminoacetone synthase, Glycine acetyltransferase
Recombinant Human GCAT protein (denatured) is a Human Full Length protein, in the 22 to 419 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl
Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
GCAT also known as glycine C-acetyltransferase functions as a mitochondrial enzyme involved in glycine metabolism. It has a molecular mass of approximately 44 kDa. Researchers often find GCAT expressed in the liver where it plays a significant role in metabolic processes related to amino acid synthesis and catabolism. Being predominantly cytosolic GCAT contributes to the detoxification pathways by participating in the conversion of glycine to other metabolites.
In glycine cleavage system GCAT operates as part of a complex essential for the regulation of amino acid levels. The enzyme accepts substrates from reactions facilitated by other components such as T-protein and P-protein and is vital in maintaining the balance of glycine and other amino acids within the cell. Dysfunction in any part of this system can result in elevated levels of toxic metabolic intermediates leading to cellular stress and potential tissue damage.
GCAT is an integral element in the mitochondrial glycine cleavage system linking it to broader metabolic pathways such as the Krebs cycle and oxidative phosphorylation. This position between pathways underlines its connection with proteins such as glycine dehydrogenase and aminomethyltransferase. This interconnectedness suggests that imbalances involving GCAT can disrupt metabolic homeostasis influencing energy production at the cellular level.
Defects or dysregulation in GCAT activity link to various metabolic conditions including nonketotic hyperglycinemia and liver diseases. Patients with nonketotic hyperglycinemia show accumulation of glycine leading to neurological issues conditions typically associated with deficiencies in glycine metabolism enzymes like P-protein. In the context of liver diseases alterations in GCAT's function affect the liver's ability to process nitrogen highlighting its importance in liver homeostasis and function.
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15% SDS-PAGE analysis of ab156971 (3 µg).
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