Aspartate decarboxylase
From Proteopedia
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'''Aspartate 1-decarboxylase''' or '''aspartate α-decarboxylase''' (AADC) catalyzes the conversion of L-aspartate to β-alanine and CO2.<ref>PMID:14633979</ref> '''Aspartate 4-decarboxylase''' or '''aspartate β-decarboxylase''' (ABDC) catalyzes the conversion of L-aspartate to L-alanine and CO2.<ref>PMID:19368885</ref> 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. | '''Aspartate 1-decarboxylase''' or '''aspartate α-decarboxylase''' (AADC) catalyzes the conversion of L-aspartate to β-alanine and CO2.<ref>PMID:14633979</ref> '''Aspartate 4-decarboxylase''' or '''aspartate β-decarboxylase''' (ABDC) catalyzes the conversion of L-aspartate to L-alanine and CO2.<ref>PMID:19368885</ref> 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. | ||
| + | *<scene name='59/592671/Cv/2'>Pyruvate binding site</scene> of AADC (PDB code [[1uhd]]). | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:31, 8 December 2015
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3D structures of aspartate decarboxylase
Updated on 08-December-2015
References
- ↑ 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
