Ambler R P, Daniel M, Fleming J, Hermoso J M, Pang C, Waley S G
FEBS Lett. 1985 Sep 23;189(2):207-11. doi: 10.1016/0014-5793(85)81024-3.
The amino acid sequence of the zinc-requiring beta-lactamase II from Bacillus cereus strain 569 has been determined. It consists of a single polypeptide chain of 227 residues. It is the only example so far fully characterized of a class B beta-lactamase, and is structurally and mechanistically distinct from both the widely distributed class A beta-lactamases (such as the Escherichia coli RTEM enzyme) and from the chromosomally encoded class C enzymes from Gram-negative bacteria.
蜡样芽孢杆菌569菌株中需锌β-内酰胺酶II的氨基酸序列已被确定。它由一条含227个残基的单一多肽链组成。它是目前已完全表征的B类β-内酰胺酶的唯一实例,在结构和作用机制上与广泛分布的A类β-内酰胺酶(如大肠杆菌RTEM酶)以及革兰氏阴性菌中染色体编码的C类酶均不同。