Structural highlights
Function
[DGDA_BURCE] The dialkylglycine decarboxylase is of interest because it normally catalyzes both decarboxylation and amino transfer. It may be more properly described as a decarboxylating aminotransferase rather than an aminotransferring decarboxylase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an alpha helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.
Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites.,Toney MD, Hohenester E, Cowan SW, Jansonius JN Science. 1993 Aug 6;261(5122):756-9. PMID:8342040[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Toney MD, Hohenester E, Cowan SW, Jansonius JN. Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science. 1993 Aug 6;261(5122):756-9. PMID:8342040
