Péduzzi J, Barthélémy M, Tiwari K, Mattioni D, Labia R
Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique Unité de Recherche Associée, Paris, France.
Antimicrob Agents Chemother. 1989 Dec;33(12):2160-3. doi: 10.1128/AAC.33.12.2160.
Tryptic peptides of the novel ceftazidimase CAZ-5 were sequenced by manual Edman degradation and aligned according to strong homology (more than 98%) with SHV-1 and SHV-2 beta-lactamase sequences. CAZ-5 differed from SHV-1 by five amino acid substitutions. Unusually high activity of CAZ-5 towards ceftazidime was imputed to substitution of a Lys for a Glu at position 214 of the mature protein.
新型头孢他啶酶CAZ-5的胰蛋白酶肽段通过手动埃德曼降解法进行测序,并根据与SHV-1和SHV-2β-内酰胺酶序列的高度同源性(超过98%)进行比对。CAZ-5与SHV-1有五个氨基酸取代差异。CAZ-5对头孢他啶的异常高活性归因于成熟蛋白214位的赖氨酸被谷氨酸取代。