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From Genome to Proteome to Elucidation of Reactions for All Eleven Known Lytic Transglycosylases from Pseudomonas aeruginosa
Author(s) -
Lee Mijoon,
Hesek Dusan,
Dik David A.,
Fishovitz Jennifer,
Lastochkin Elena,
Boggess Bill,
Fisher Jed F.,
Mobashery Shahriar
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201611279
Subject(s) - peptidoglycan , lytic cycle , pseudomonas aeruginosa , cell wall , bacterial cell structure , bacteria , chemistry , biochemistry , proteome , enzyme , cleavage (geology) , microbiology and biotechnology , biology , genetics , virus , paleontology , fracture (geology)
An enzyme superfamily, the lytic transglycosylases (LTs), occupies the space between the two membranes of Gram‐negative bacteria. LTs catalyze the non‐hydrolytic cleavage of the bacterial peptidoglycan cell‐wall polymer. This reaction is central to the growth of the cell wall, for excavating the cell wall for protein insertion, and for monitoring the cell wall so as to initiate resistance responses to cell‐wall‐acting antibiotics. The nefarious Gram‐negative pathogen Pseudomonas aeruginosa encodes eleven LTs. With few exceptions, their substrates and functions are unknown. Each P. aeruginosa LT was expressed as a soluble protein and evaluated with a panel of substrates (both simple and complex mimetics of their natural substrates). Thirty‐one distinct products distinguish these LTs with respect to substrate recognition, catalytic activity, and relative exolytic or endolytic ability. These properties are foundational to an understanding of the LTs as catalysts and as antibiotic targets.