A Possible Interaction or A Similarity between the Mechanism of Action of the Arylamidase Enzyme and the Ferripyoverdine Receptor Genes in Pseudomonas aeruginosa

The essential element iron is relatively soluble in nature and because of its relative solubility, gram negative bacteria, for example, Pseudomonas aeruginosa synthesizes a low molecular weight compound called Pyoverdine. Pyoverdine enables P. aeruginosa trap iron from the external environment into the internal milieu. Iron bound to these compounds are recognized at the outer membrane by the ferripyoverdine receptor genes. The ferripyoverdine receptors help in channeling iron into the internal milieu for use by P. aeruginosa. The Pseudomonas aeruginosa arylamidase enzyme was purified in 1971, and P. aeruginosa uses this enzyme to hydrolyze basic and neutral N-terminal amino acid residues from amino-ß-naphthylamides, dipeptide-ß- naphthylamides, and a variety of polypeptides and according to the scientists who purified this enzyme, only those substrates having an L-amino acid with an unsubstituted α-amino group as the N-terminal residue were susceptible to enzymatic hydrolysis. Based on scientific observations from my previous work titled “Ferripyoverdine receptors and general metabolism in Pseudomonas aeruginosa, Preliminary results” and the scientific research work done by other authors, I am of the opinion that the ferripyoverdine receptor gene and the arylamidase enzyme may interact or may be somewhat similar in their mechanisms of operation.