In enzymology, a 2,2-dialkylglycine decarboxylase (pyruvate) () is an enzyme that catalyzes the chemical reaction

2,2-dialkylglycine + pyruvate \rightleftharpoons dialkyl ketone + CO₂ + L-alanine

Thus, the two substrates of this enzyme are 2,2-dialkylglycine and pyruvate, whereas its 3 products are dialkyl ketone, CO₂, and L-alanine.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2,2-dialkylglycine carboxy-lyase (amino-transferring L-alanine-forming). Other names in common use include dialkyl amino acid (pyruvate) decarboxylase, alpha-dialkyl amino acid transaminase, 2,2-dialkyl-2-amino acid-pyruvate aminotransferase, L-alanine-alpha-ketobutyrate aminotransferase, dialkylamino-acid decarboxylase (pyruvate), and 2,2-dialkylglycine carboxy-lyase (amino-transferring). It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , and .

References