GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

TableEdit

Jump to: navigation, search

PMID:17693492

You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki

See Help for Help on this wiki. See the documentation for how to use the table editor

Citation

Giles, TN and Graham, DE (2007) Characterization of an acid-dependent arginine decarboxylase enzyme from Chlamydophila pneumoniae. J. Bacteriol. 189:7376-83

Abstract

Genome sequences from members of the Chlamydiales encode diverged homologs of a pyruvoyl-dependent arginine decarboxylase enzyme that nonpathogenic euryarchaea use in polyamine biosynthesis. The Chlamydiales lack subsequent genes required for polyamine biosynthesis and probably obtain polyamines from their host cells. To identify the function of this protein, the CPn1032 homolog from the respiratory pathogen Chlamydophila pneumoniae was heterologously expressed and purified. This protein self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alphabeta)(3) complex. The mature enzyme specifically catalyzed the decarboxylation of L-arginine, with an unusually low pH optimum of 3.4. The CPn1032 gene complemented a mutation in the Escherichia coli adiA gene, which encodes a pyridoxal 5'-phosphate-dependent arginine decarboxylase, restoring arginine-dependent acid resistance. Acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system. These genes are the first evidence that obligately intracellular chlamydiae may encounter acidic conditions. Alternatively, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase.

Links

PubMed PMC2168457 Online version:10.1128/JB.00772-07

Keywords

Acids/pharmacology; Adaptation, Physiological/genetics; Amino Acid Sequence; Anti-Bacterial Agents/pharmacology; Arginine/metabolism; Carboxy-Lyases/chemistry; Carboxy-Lyases/genetics; Carboxy-Lyases/metabolism; Chlamydiales; Chlamydophila pneumoniae/enzymology; Cloning, Molecular; Drug Resistance, Bacterial/genetics; Drug Resistance, Bacterial/physiology; Enzyme Stability; Escherichia coli/drug effects; Escherichia coli/genetics; Gene Deletion; Genetic Complementation Test; Hydrogen-Ion Concentration; Molecular Sequence Data; Protein Subunits; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Alignment; Substrate Specificity

public



Cancel