Category:Complex:aspartate 1-decarboxylase
About
Description (originally from EcoCyc[1]) aspartate 1-decarboxylase
Comments (originally from EcoCyc[1]) Aspartate 1-decarboxylase is responsible for the synthesis of β-alanine, which is needed in the biosynthesis of panthothenate. This enzyme is one of a small class of enzymes that use a covalently bound pyruvoyl prosthetic group. The pyruvoyl group is thought to act analogously to pyridoxal phosphate cofactor by forming a Schiff base with the amino group of the substrate and then serving as an electron sink to facilitate the decarboxylation [2][3].
Pyruvoyl-containing enzymes are expressed as a zymogen which is processed post-translationally by a self-maturation cleavage called serinolysis. In this process the pyruvoul group is formed from a serine residue, splitting the presursor protein into two parts which become the α and β subunits. In some cases additional subunits may be involved.
References
- ↑ 1.0 1.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Diaz, E & Anton, DL (1991) Alkylation of an active-site cysteinyl residue during substrate-dependent inactivation of Escherichia coli S-adenosylmethionine decarboxylase. Biochemistry 30 4078-81 PubMed
- ↑ Xiong, H & Pegg, AE (1999) Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J. Biol. Chem. 274 35059-66 PubMed
This category currently contains no pages or media.
