Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii
Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii
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DOI：
10.1128/aac.49.10.4174-4179.2005
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发表时间：
2005-10-01
影响因子：
4.9
通讯作者：
Nordmann, P
中科院分区：
文献类型：
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作者：
Héritier, C;Poirel, L;Nordmann, P
染色体编码的苯唑西林酶 OXA-69 是从鲍曼不动杆菌 AYE 中鉴定出来的。 P-内酰胺酶 OXA-69 与最近描述的鲍曼不动杆菌的 OXA-51 酶具有 97% 的氨基酸同一性，与碳青霉烯水解苯唑西林酶 OXA-24 和 OXA-23 分别具有 62% 和 56% 的氨基酸同一性。纯化的 OXA-69 的生化特征显示其具有窄谱水解特征，但含有低水平的亚胺培南和美罗培南。通过 PCR 和测序，在所有测试的鲍曼不动杆菌菌株 (n = 12) 中鉴定出 bla(OXA-69) 样基因，表明这种苯唑西林酶在该物种中天然存在。
A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. P-Lactamase OXA-69 shared 97% amino acid identity with the recently described OXA-51 enzyme of A. baumannii and 62 and 56% amino acid identity with the carbapenem-hydrolyzing oxacillinases OXA-24 and OXA-23, respectively. Biochemical characterization of the purified OXA-69 revealed a narrow-spectrum hydrolysis profile but including, at a low level, imipenem and meropenem. By PCR and sequencing bla(OXA-69)-like genes were identified in all A. baumannii strains tested (n = 12), suggesting that this oxacillinase is naturally occurring in that species.