The
enzyme 2,2-dialkylglycine decarboxylase (pyruvate) ()
catalyzes
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the
chemical reaction
:2,2-dialkylglycine + pyruvate
dialkyl ketone + CO
2 + L-alanine
This enzyme belongs to the family of
lyase
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. ...
s, 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
*
EC 4.1.1
Pyridoxal phosphate enzymes
Enzymes of known structure
{{4.1-enzyme-stub