Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023241 (Legionella)
 6,990 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzyme activities of four strains of Legionella pneumophilia were investigated by using the API ZYM system (API System S.A., F-38390 Montalieu Vercieu, France) and synthetic substrates. Aminopeptidases were detected specifically against L-alanine, L-arginine, L-aspartic acid, L-cystine, L-glutaminic acid, glycine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-tryptophan, L-tyrosine, and L-valine. Furthermore, the bacteria possesses esterase activity splitting propionate, butyrate, caproate, caprylate, and caprate, but not laurate, myristate, palmitate, and stearate, esters. The enzymes studies were inhibited partially by aprotinin. No inhibition of phosphatase (pH range, 5.4 to 8.5) or of phosphoamidase was observed. Activities of arylsulfatase, chymotrypsin, trypsin, and glycosidases could not be detected.
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PMID:Enzymatic profile of Legionella pneumophilia. 616 35

The API ZYM system was used to investigate enzymatic activities of Legionella pneumophila and other Legionella-like organisms. Leucine aminopeptidase, alkaline and acid phosphatase, butyrate and caprylate esterase, and phosphoamidase activities were consistently detected in all strains tested. No evidence of myristate lipase, trypsin, chymotrypsin, or glycosidase activity was found.
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PMID:Enzymatic activities of Legionella pneumophila and Legionella-like organisms. 718 5

The culture conditions of Afipia felis, A. broomeae, A. clevelandensis and three unnamed Afipia genospecies were investigated on BCY agar supplemented with different substances known as growth factors of Legionella spp. and, furthermore, with sodium chloride and other salts. The organisms were found to be susceptible to a certain degree to byproducts of the autoclaving which are scavenged by activated by charcoal. Growth was weakly enhanced by ferric pyrophosphate, cystein.HCl, and alpha-ketoglutarate. These substances are no obligatory growth factors. The optimal pH value was about 6.8. Afipia spp. showed a strong susceptibility to NaCl and other salts. They possess phosphatase, phosphoamidase, phosphodiesterase, a weak sulfatase, glycine aminopeptidase, and L-lysine aminopeptidase. The strains differed with regard to other proteases and aminopeptidases. The decimal reduction times of A. felis at 55 degrees C and 60 degrees C were 11 min, < 1 min, respectively.
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PMID:Investigations of culture and properties of Afipia spp. 773 25