Müller H E
J Clin Microbiol. 1981 Mar;13(3):423-6. doi: 10.1128/jcm.13.3.423-426.1981.
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.
采用API ZYM系统（法国蒙塔利厄韦尔西厄市API System S.A.公司，邮编F - 38390）和合成底物对四株嗜肺军团菌的酶活性进行了研究。特异性检测了针对L - 丙氨酸、L - 精氨酸、L - 天冬氨酸、L - 胱氨酸、L - 谷氨酸、甘氨酸、L - 组氨酸、L - 异亮氨酸、L - 亮氨酸、L - 赖氨酸、L - 蛋氨酸、L - 苯丙氨酸、L - 色氨酸、L - 酪氨酸和L - 缬氨酸的氨肽酶。此外，该细菌具有酯酶活性，可分解丙酸酯、丁酸酯、己酸酯、辛酸酯和癸酸酯，但不能分解月桂酸酯、肉豆蔻酸酯、棕榈酸酯和硬脂酸酯。所研究的酶受到抑肽酶的部分抑制。未观察到磷酸酶（pH范围为5.4至8.5）或磷酸酰胺酶受到抑制。未检测到芳基硫酸酯酶、胰凝乳蛋白酶、胰蛋白酶和糖苷酶的活性。
