肺炎克雷伯菌的K1β-内酰胺酶。
The K1 beta-lactamase of Klebsiella pneumoniae.
作者信息
Joris B, De Meester F, Galleni M, Frère J M, Van Beeumen J
出版信息
Biochem J. 1987 Apr 15;243(2):561-7. doi: 10.1042/bj2430561.
Abstract
beta-Lactamase K1 was purified from Klebsiella pneumoniae SC10436. It is very similar to the enzyme produced by Klebsiella aerogenes 1082E and described by Emanuel, Gagnon & Waley [Biochem. J. (1986) 234, 343-347]. An active-site peptide was isolated after labelling of the enzyme with tritiated beta-iodopenicillanate. A cysteine residue was found just before the active-site serine residue. This result could explain the properties of the enzyme after modification by thiol-blocking reagents. The sequence of the active-site peptide clearly established the enzyme as a class A beta-lactamase.
摘要
β-内酰胺酶K1是从肺炎克雷伯菌SC10436中纯化得到的。它与产气克雷伯菌1082E产生的、由伊曼纽尔、加尼翁和韦利描述的酶非常相似[《生物化学杂志》（1986年）234卷，343 - 347页]。在用氚标记的β-碘青霉素酸标记该酶后，分离出了一个活性位点肽段。在活性位点丝氨酸残基之前发现了一个半胱氨酸残基。这一结果可以解释该酶经硫醇阻断试剂修饰后的特性。活性位点肽段的序列明确证实该酶为A类β-内酰胺酶。
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