一种真菌几丁质脱乙酰酶的一级结构揭示了两种细菌基因产物的功能。
The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products.
作者信息
Kafetzopoulos D, Thireos G, Vournakis J N, Bouriotis V
机构信息
Institute of Molecular Biology and Biotechnology, Crete, Greece.
出版信息
Proc Natl Acad Sci U S A. 1993 Sep 1;90(17):8005-8. doi: 10.1073/pnas.90.17.8005.
Abstract
Chitin deacetylase (EC 3.5.1.41) hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. A cDNA to the Mucor rouxii mRNA encoding chitin deacetylase was isolated, characterized, and sequenced. Protein sequence comparisons revealed significant similarities of the fungal chitin deacetylase to rhizobial nodB proteins and to an uncharacterized protein encoded by a Bacillus stearothermophilus open reading frame. These data suggest the functional homology of these evolutionarily distant proteins. NodB is a chitooligosaccharide deacetylase essential for the biosynthesis of the bacterial nodulation signals, termed Nod factors. The observed similarity of chitin deacetylase to the B. stearothermophilus gene product suggests that this gene encodes a polysaccharide deacetylase.
摘要
几丁质脱乙酰酶（EC 3.5.1.41）可水解几丁质中N-乙酰-D-葡萄糖胺残基的N-乙酰氨基基团。分离、鉴定并测序了编码鲁氏毛霉几丁质脱乙酰酶的mRNA的cDNA。蛋白质序列比较显示，真菌几丁质脱乙酰酶与根瘤菌nodB蛋白以及嗜热脂肪芽孢杆菌开放阅读框编码的一种未鉴定蛋白具有显著相似性。这些数据表明这些在进化上距离遥远的蛋白质具有功能同源性。NodB是一种几丁寡糖脱乙酰酶，对称为根瘤因子的细菌结瘤信号的生物合成至关重要。观察到的几丁质脱乙酰酶与嗜热脂肪芽孢杆菌基因产物的相似性表明该基因编码一种多糖脱乙酰酶。
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