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Transaminases require the coenzyme pyridoxal phosphate, which is converted into pyridoxamine in the first half-reaction, when an amino acid is converted into a keto acid. Enzyme-bound pyridoxamine in turn reacts with pyruvate , oxaloacetate , or alpha-ketoglutarate , giving alanine , aspartic acid , or glutamic acid , respectively.
In medicine, the presence of elevated transaminases, commonly the transaminases alanine transaminase (ALT) and aspartate transaminase (AST), may be an indicator of liver dysfunction. [ 1 ] [ 2 ] Other terms include transaminasemia , [ 3 ] and elevated liver enzymes (though they are not the only enzymes in the liver).
The liver transaminases aspartate transaminase (AST or SGOT) and alanine transaminase (ALT or SGPT) are useful biomarkers of liver injury in a patient with some degree of intact liver function. [2] [3] [4] Most liver diseases cause only mild symptoms initially, but these diseases must be detected early. Hepatic (liver) involvement in some ...
Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases. α-ketoglutarate acts as the predominant amino-group acceptor and produces glutamate as the new amino acid. Aminoacid + α-ketoglutarate ↔ α-keto acid + glutamate
Alanine transaminase (ALT), also known as alanine aminotransferase (ALT or ALAT), formerly serum glutamate-pyruvate transaminase (GPT) or serum glutamic-pyruvic transaminase (SGPT), is a transaminase enzyme (EC 2.6.1.2) that was first characterized in the mid-1950s by Arthur Karmen and colleagues. [1]
The proportion of AST to ALT in hepatocytes is about 2.5:1, but because AST is removed from serum by the liver sinusoidal cells twice as quickly (serum half-life t 1/2 = 18 hr) compared to ALT (t 1/2 = 36 hr), so the resulting serum levels of AST and ALT are about equal in healthy individuals, resulting in a normal AST/ALT ratio around 1.
In enzymology, a D-amino-acid transaminase (EC 2.6.1.21) is an enzyme that catalyzes the chemical reaction: . D-alanine + 2-oxoglutarate pyruvate + D-glutamate. Thus, the two substrates of this enzyme are D-alanine and 2-oxoglutarate, whereas its two products are pyruvate and D-glutamate.
Aminotransferases (transaminases) in general have been used to create unnatural amino acids, important building blocks for peptidomimetic drugs and agricultural products. BCAT from E. coli is typically engineered to be overexpressed and extracted from whole cells to be used for chemical synthesis. [ 33 ]