Aspartate aminotransferase

The Uses of Aspartate aminotransferase

Converts L-aspartate and alpha-ketoglutarate to oxaloacetate and L-glutamate

Definition

An enzyme that catalyzes reversibly the transfer of an amino group from glutamic acid to oxaloacetic acid, yielding α-ketoglutaric acid and aspartic acid. The codons for aspartate are GAC and GAU.

General Description

Glutamic-Oxalacetic Transaminase is found in all tissues and is predominant in the liver and skeletal muscle. It is a prototype of fold-type I pyridoxal 5′-phosphate (PLP)-enzymes. Glutamic-oxalacetic transaminase is a homodimer containing large and small domains in each subunit.

Biochem/physiol Actions

Glutamic-oxalacetic transaminase or aspartate aminotransferase (AAT) catalyzes the interconversion of L-aspartate and α-ketoglutarate with oxalacetate and L-glutamate. This reversible transaminase reaction is dependent on pyridoxal 5′-phosphate (PLP). Glutamic-oxalacetic transaminase maintains the nitrogen currency for metabolism by generating L-glutamate. Elevated serum levels of glutamic-oxalacetic transaminase are indicated in myocardial infarction, liver diseases, and some renal diseases.