Open AccessPeptidase N and alanyl‐peptide transport in Pseudomonas aeruginosa
Author(s) -
Hulen Christian,
Goffic François
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02709.x
Subject(s) - permease , tripeptide , pseudomonas aeruginosa , biochemistry , alanine , dipeptide , peptide , bacteria , chemistry , biology , amino acid , mutant , genetics , gene
Alanine dipeptides normally penetrate into Pseudomonas aeruginosa by the way of two transport systems. In peptidase N‐deficient mutants, dialanine is unable to use its low affinity transport system. Uptake competition showed that this system harboured a permease common to the transport of the amino acid alanine. This permease permits the penetration of both alanine and alanyl peptides uniquely in the presence of active peptidase N. The uptake of trialanine is independent of the presence of active peptidase N inside bacteria despite the fact that hydrolysis of this tripeptide absolutely requires this activity.