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Glutamine—pyruvate transaminase

From Wikipedia, the free encyclopedia

glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction[1][2]

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Reversible left-right reaction arrow
 
 
 
2D representation of the chemical structure of Q27104163.
2-oxoglutaramic acid
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The two substrates of this enzyme characterised from rat liver are L-glutamine and pyruvic acid. Its products are 2-oxoglutaramic acid and L-alanine.[1]

This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:pyruvate aminotransferase. Other names in common use include glutaminase II, L-glutamine transaminase L, and glutamine-oxo-acid transaminase. It uses pyridoxal phosphate as a cofactor.[3]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1V2D​, PDB: 1V2E​, and PDB: 1V2F​.

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