THE STRUCTURE OF BETA-LACTAMASES
THE STRUCTURE OF BETA-LACTAMASES
复制标题
DOI：
10.1098/rstb.1980.0049
复制
发表时间：
1980-01-01
影响因子：
6.3
通讯作者：
AMBLER, RP
中科院分区：
文献类型：
--
作者：
AMBLER, RP
β-内酰胺酶广泛分布于革兰氏阳性菌和革兰氏阴性菌中。它们都通过打开β-内酰胺环来灭活青霉素和头孢菌素。酶的许多品种可以根据其催化和分子特性来区分，但只有氨基酸序列测定才能提供分子系统发育所依据的信息。目前的证据表明β-内酰胺酶具有多系起源。目前已知氨基酸序列的所有β-内酰胺酶都属于一个同源组，这里称为A类酶。 B 类由机制上不同的蜡样芽孢杆菌β-内酰胺酶 II 组成，初步部分序列分析表明其在结构上与 A 类酶无关。据预测，序列分析将表明需要创建更多类别来解释具有独特分子和机械特性的特定 β-内酰胺酶。
The β-lactamases are widely distributed in both Gram-positive and Gram-negative bacteria. They all inactivate penicillins and cephalosporins by opening the β-lactam ring. Many varieties of the enzyme can be distinguished on the basis of their catalytic and molecular properties, but only amino acid sequence determination gives information upon which a molecular phylogeny can be based. The present evidence suggests that the β-lactamases have a polyphyletic origin. All the β-lactamases of currently known amino acid sequence belong to one homology group, here called class A enzymes. Class B consists of the mechanistically distinctBacillus cereusβ-lactamase II, which preliminary partial sequence analysis suggests to be structurally unrelated to the class A enzymes. It is predicted that sequence analysis will show that further classes will need to be created to account for particular β-lactamases of distinctive molecular and mechanistic properties.