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
2,2-dialkylglycine decarboxylase (pyruvate)
Identifiers
EC number4.1.1.64
CAS number9032-17-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

gollark: HAZF 44 545 4AS6 F4\\da [unicode decode error]
gollark: Pyrust.
gollark: Haskthon.
gollark: ++exec```pyprint str(bin(int("this is very cool and fun!".encode("hex"), 16)))[2:].replace("0", "haskell").replace("1", "rust")```
gollark: ++exec```pyprint str(bin(int("abcd".encode("hex"), 16)))[2:].replace("0", "haskell").replace("1", "rust")```

References
    • Bailey GB, Dempsey WB (1967). "Purification and properties of an alpha-dialkyl amino acid transaminase". Biochemistry. 6 (5): 1526–1533. doi:10.1021/bi00857a039.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.