2,2-dialkylglycine decarboxylase (pyruvate)

In enzymology, a 2,2-dialkylglycine decarboxylase (pyruvate) (EC 4.1.1.64) is an enzyme that catalyzes the chemical reaction

2,2-dialkylglycine + pyruvate 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

Structural studies

As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 1D7R, 1D7S, 1D7U, 1D7V, 1DGD, 1DGE, 1DKA, 1M0N, 1M0O, 1M0P, 1M0Q, 1Z3Z, 1ZC9, 1ZOB, 1ZOD, and 2DKB.