Journal article

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

Abstract

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..

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University of Melbourne Researchers