Function
Aspartate 1-decarboxylase or aspartate α-decarboxylase (AADC) catalyzes the conversion of L-aspartate to β-alanine and CO2.[1] Aspartate 4-decarboxylase or aspartate β-decarboxylase (ABDC) catalyzes the conversion of L-aspartate to L-alanine and CO2.[2] AADC is a pyruvate-dependent enzyme which is synthesized as an inactive protein. The AADC inactive precursor is cleaved to the active α and β subunits. ABDC is a pyridoxal-5’-phosphate (PLP)-dependent enzyme.
3D structures of aspartate decarboxylase
Aspartate decarboxylase 3D structures
- ↑ Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL. Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase. EMBO J. 2003 Dec 1;22(23):6193-204. PMID:14633979 doi:10.1093/emboj/cdg575
- ↑ Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH. Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase. Structure. 2009 Apr 15;17(4):517-29. PMID:19368885 doi:10.1016/j.str.2009.02.013
- ↑ Lee BI, Suh SW. Crystal structure of the schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase. J Mol Biol. 2004 Jun 25;340(1):1-7. PMID:15184017 doi:10.1016/j.jmb.2004.04.049
