methionine-glyoxylate transaminase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine. [EC:2.6.1.73, RHEA:22884]

Methionine-glyoxylate transaminase activity is a catalytic function that transfers an amino group from L-methionine to glyoxylate, generating pyruvate and L-serine. This reaction plays a crucial role in the metabolism of both methionine and glycine, two essential amino acids. The enzyme responsible for this activity, known as methionine-glyoxylate transaminase (MGT), is a member of the pyridoxal phosphate-dependent transaminase family.

MGT catalyzes the reversible conversion of L-methionine and glyoxylate to pyruvate and L-serine, with pyridoxal phosphate (PLP) as a cofactor. The reaction proceeds through a series of steps involving Schiff base formation between the enzyme and PLP, followed by transamination, decarboxylation, and hydrolysis. The amino group from L-methionine is transferred to PLP, forming a Schiff base intermediate. This intermediate undergoes decarboxylation, releasing carbon dioxide and forming a new Schiff base with the carbon adjacent to the carbonyl group. Finally, the amino group is transferred to glyoxylate, resulting in the formation of pyruvate and L-serine.

The activity of MGT is essential for maintaining amino acid homeostasis and regulating metabolic pathways. In addition to its role in methionine and glycine metabolism, MGT has been implicated in other metabolic processes, including gluconeogenesis and detoxification.

In conclusion, methionine-glyoxylate transaminase activity is a crucial enzymatic process that contributes to the metabolism of essential amino acids and plays a vital role in maintaining metabolic balance in living organisms.'
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Proteins (1)

Compounds (3)