Berdal B P, Bøvre K, Olsvik O, Omland T
J Clin Microbiol. 1983 Jun;17(6):970-4. doi: 10.1128/jcm.17.6.970-974.1983.
Some Legionella strains possess a strong extracellular proline-specific endopeptidase (PSE) activity. Using an enlarged selection of chromogenic peptides representing a variety of N-terminal amino-acids binding to a -prolyl-proline, paranitroanilide chain, PSE activity of Legionella and Flavobacterium strains was examined. Differences in PSE activity emphasized the importance of the chemical structure at the nonchromogenic end of the peptide substrates. There seem to be distinct patterns of N-terminal specificity of PSE in the two bacterial groups.
一些军团菌菌株具有很强的细胞外脯氨酸特异性内肽酶(PSE)活性。使用大量代表与对硝基苯胺链相连的各种N端氨基酸的生色肽,检测了军团菌和黄杆菌菌株的PSE活性。PSE活性的差异突出了肽底物非生色端化学结构的重要性。这两类细菌的PSE在N端特异性方面似乎存在明显模式。