ISOLATION AND CHARACTERIZATION OF A PENICILLINASE FROM PSEUDOMONAS-CEPACIA 249
ISOLATION AND CHARACTERIZATION OF A PENICILLINASE FROM PSEUDOMONAS-CEPACIA 249
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DOI：
10.1128/aac.32.6.838
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发表时间：
1988-06-01
影响因子：
4.9
通讯作者：
CHIN, NX
中科院分区：
文献类型：
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作者：
PRINCE, A;WOOD, MS;CHIN, NX
洋葱假单胞菌具有可诱导的β-内酰胺酶，其具有分解代谢β-内酰胺酶的新能力。内酰胺化合物。编码这种酶的基因，佩纳，是从洋葱疫霉249的基因组文库中克隆到广宿主范围粘粒pLAFR上的。这将佩纳基因与编码第二个β-半乳糖苷酶的基因分离。第249章.佩纳的表达在大肠杆菌宿主菌株中可被低水平的青霉素诱导。这种分子量为33，500的酶具有不受克拉维酸或舒巴坦抑制的青霉素酶活性，对哌拉西林和阿洛西林具有高度活性。与其它诱导型β-作为革兰氏阴性菌产生的内酰胺酶，佩纳酶具有许多与粪产碱杆菌产生的青霉素酶相似的性质。与铜绿假单胞菌产生的ampC型头孢菌素酶不同。
Pseudomonas cepacia has an inducible .beta.-lactamase which is responsible for its novel ability to catabolize .beta.-lactam compounds. The gene encoding this enzyme, penA, was cloned from a genomic library of P. cepacia 249 on the broad-host-range cosmid pLAFR. This separated the penA gene from the gene encoding a second .beta.-lactamase in P. cepacia 249. Expression of penA was inducible in an Escherichia coli host strain by low levels of penicillin. The 33,500-molecular-weight enzyme had penicillinase activity not inhibited by clavulanic acid or sulbactam and was highly active against piperacillin and azlocillin. In comparison with other inducible .beta.-lactamases produced by gram-negative organisms, the penA enzyme had many properties which were similar to those of the penicillinase produced by Alcaligenes faecalis. It was unlike the ampC-type cephalosporinase produced by Pseudomonas aeruginosa.