L-cysteine transaminase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate. [RHEA:17441]

L-cysteine transaminase activity is a biochemical process that catalyzes the transfer of an amino group from L-cysteine to an α-keto acid, typically α-ketoglutarate. This reaction results in the formation of pyruvate and L-glutamate. The enzyme responsible for this activity is called cysteine aminotransferase (CAT), also known as cysteine transaminase.

CAT plays a crucial role in the metabolism of cysteine, a sulfur-containing amino acid essential for various cellular processes. It facilitates the removal of the amino group from L-cysteine, which can then be further metabolized to pyruvate or used in other metabolic pathways.

The reaction mechanism of L-cysteine transaminase activity involves the formation of a Schiff base intermediate between the amino group of L-cysteine and the pyridoxal phosphate (PLP) cofactor bound to the enzyme. This Schiff base is then converted to a quinonoid intermediate, which is subsequently attacked by the α-keto acid, leading to the formation of pyruvate and L-glutamate.

L-cysteine transaminase activity is highly regulated and influenced by various factors, including the availability of substrates, cofactors, and inhibitors. Dysregulation of CAT activity has been linked to several human diseases, including cancer, neurodegenerative disorders, and metabolic diseases. Therefore, understanding the molecular function of L-cysteine transaminase activity is crucial for developing novel therapeutic strategies for these diseases.'
"

Proteins (2)

Compounds (23)