Proteinases of Legionella: Phenylalanineaminopeptidase of L. pneumophila
Gul'nik, Sergei V. and Yusupova, Margarita P. and Lavrenova, Galina I. and Tartakovsky, Igor S. and Prozorovsky, Sergei V. and Stepanov, Valentin M.,, 132, 387-392 (1986),
doi = https://doi.org/10.1099/00221287-132-2-387,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= Summary: Phenylalanineaminopeptidase was isolated and purified from the culture filtrate of Legionella pneumophila by affinity chromatography on O-tert-butyl-l-threonyl-l-phenylalanyl-l-prolyl-glycyl-aminosilochrom and by gel-filtration; a 401-fold purification with a yield of 18% was achieved. The enzyme was a metalloenzyme with a molecular weight of 35000 and a pI of 5.8. It was stable at pH 7–9 and had an activity optimum in the range of pH 8–9.5 with l-phenylalanine p-nitroanilide as substrate. Enzyme activity was highest towards the latter compound, substantially lower towards l-leucine p-nitroanilide and only marginal towards other p-nitroanilides. Besides phenylalanineaminopeptidase, a metalloproteinase and a serine proteinase were also detected in L. pneumophila culture filtrate.,
language=,
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