Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent decarboxylase in beta-alanine production
Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme L-aspartate decarboxylase (ADC), EC:18.104.22.168 which requires a pyruvoyl group for its activity. The pyruvoyl cofactor is covalently bound to the enzyme. The protein is synthesized as a proenzyme and cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment), and the pyruvoyl group. Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The active site of the tetrameric enzyme is located at the interface of two subunits, with a Lysine and a Histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit. This alignment model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase.
Comment:Gly23-Ser24 form the cofactor pyruvoyl by intramolecular non-hydrolytic serinolysis
Comment:Structures demonstrating the active configuration with the covalently bound cofactor are not included in this alignment model, as they are proteolytically cleaved and split into two smaller chains, represented by the stretches in this alignment which are N- and C-terminal to Gly23-Ser24
Structure:1PQH: A Ser24Thr mutant of aspartate 1-decarboxylase from Escherichia coli binds malonic acid, indicating the location of the substrate in the native active enzyme - View structure with Cn3D