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2,2 dialkylglycine decarboxylase (pyruvate)

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EC number
  
4.1.1.64

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
9032-17-1

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

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.

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.

References

2,2-dialkylglycine decarboxylase (pyruvate) Wikipedia