VIM金属β-内酰胺酶家族的一个不同成员VIM-7的动力学特征
Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family.
作者信息
Samuelsen Ørjan, Castanheira Mariana, Walsh Timothy R, Spencer James
机构信息
Reference Centre for Detection of Antimicrobial Resistance, Department of Microbiology and Infection Control, University Hospital of North Norway, 9038 Tromsø, Norway.
出版信息
Antimicrob Agents Chemother. 2008 Aug;52(8):2905-8. doi: 10.1128/AAC.00166-08. Epub 2008 Jun 16.
Abstract
Purified recombinant VIM-7 possesses efficient penicillinase and carbapenemase activities comparable to those of VIM-2. Cephalosporinase activity was variable and generally lower than those of VIM-1 and VIM-2. A homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.
摘要
纯化的重组VIM-7具有与VIM-2相当的高效青霉素酶和碳青霉烯酶活性。头孢菌素酶活性存在差异，通常低于VIM-1和VIM-2。同源模型表明，VIM-7的酪氨酸218被苯丙氨酸取代可能是导致其对某些头孢菌素（包括头孢他啶和头孢吡肟）催化效率降低的原因。
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