Crystal Structure of the Acid-Induced Arginine Decarboxylase from Escherichia coli: Reversible Decamer Assembly Controls Enzyme Activity
Juni Andrell, Matthew G Hicks, Tracy Palmer, Elisabeth P Carpenter, So Iwata, Megan J Maher
Biochemistry | AMER CHEMICAL SOC | Published : 2009
The acid-induced arginine decarboxylase is part of an enzymatic system in Escherichia coli that contributes to making this organism acid resistant. The arginine decarboxylase is a vitamin B(6)-dependent enzyme that is active at acidic pH. It consumes a proton in the decarboxylation of arginine to agmatine, and by working in tandem with an arginine-agmatine antiporter, this enzymatic cycle protects the organism by preventing the accumulation of protons inside the cell. We have determined the structure of the acid-induced arginine decarboxylase by X-ray crystallography to 2.4 A resolution. The arginine decarboxylase structure revealed a ca. 800 kDa decamer composed as a pentamer of five homodi..View full abstract
Awarded by Medical Research Council
This work was supported by the European Union and the BBSCR. M.J.M.. is a Cancer Institute of NSW Fellow. T.P. is an MRC senior non-clinical research fellow, and M.G.H. is an MRC-supported postdoc.