Glutamic-Oxaloacetic Transaminase 1 (GOT1), also known as Aspartate Aminotransferase 1 (AST1), is a pyridoxal phosphate-dependent enzyme that plays a crucial role in amino acid metabolism and the urea and tricarboxylic acid cycles . This enzyme exists in both cytoplasmic and mitochondrial forms, with GOT1 being the cytoplasmic form .
The GOT1 gene is located on chromosome 10 in humans and is responsible for encoding the cytoplasmic form of the enzyme . The enzyme is homodimeric, meaning it consists of two identical subunits, and shows close homology to its mitochondrial counterpart, GOT2 . The protein structure of GOT1 includes binding sites for pyridoxal phosphate, which is essential for its enzymatic activity .
GOT1 catalyzes the reversible transamination reaction between glutamate and oxaloacetate to form aspartate and alpha-ketoglutarate . This reaction is vital for the metabolism of amino acids and the production of energy through the tricarboxylic acid cycle. Additionally, GOT1 plays a significant role in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis .
Elevated levels of GOT1 in the serum are often indicative of liver damage or disease, as the enzyme is released into the bloodstream when liver cells are damaged . It is commonly measured in clinical settings as part of liver function tests. Moreover, mutations in the GOT1 gene have been associated with various metabolic disorders, including Aspartate Aminotransferase, Serum Level Of, Quantitative Trait Locus 1, and Abdominal Obesity-Metabolic Syndrome 1 .
Mouse anti-human GOT1 antibodies are used extensively in research and diagnostic applications to detect and quantify the presence of GOT1 in biological samples . These antibodies are produced by immunizing mice with human GOT1 protein, leading to the generation of specific antibodies that can bind to the human enzyme. These antibodies are valuable tools in studying the expression, localization, and function of GOT1 in various biological contexts .