泡盛曲霉乙酰酯酶：酶的纯化以及基因的克隆与测序
An Aspergillus awamori acetylesterase: purification of the enzyme, and cloning and sequencing of the gene.
作者信息
Koseki T, Furuse S, Iwano K, Sakai H, Matsuzawa H
机构信息
National Research Institute of Brewing, Higashihiroshima, Japan.
出版信息
Biochem J. 1997 Sep 1;326 ( Pt 2)(Pt 2):485-90. doi: 10.1042/bj3260485.
Abstract
An inducible acetylesterase was purified from the culture medium of Aspergillus awamori strain IFO4033 growing on wheat-bran culture by ion-exchange, gel-filtration and hydrophobic-interaction chromatographies. The purified enzyme had an Mr of 31000 and contained Asn-linked oligosaccharides. The enzyme liberated acetic acid from wheat bran, hydrolysed only alpha-naphthyl acetate and propionate when aromatic esters were used for the substrate, and was tentatively classified as a carboxylic esterase (EC 3.1.1.1). The gene encoding acetylesterase was cloned and sequenced. The deduced amino acid sequence showed that acetylesterase was produced as a 304-amino-acid-residue precursor, which was converted post-translationally into a 275-amino-acid-residue mature protein. Part of the sequence of acetylesterase was similar to the region near the active-site serine of lipases of Geotrichum candidum and Candida cylindracea. A unique site of putative Asn-linked oligosaccharides was presented.
摘要
通过离子交换、凝胶过滤和疏水相互作用色谱法，从在麦麸培养基上生长的泡盛曲霉IFO4033菌株的培养基中纯化出一种可诱导的乙酰酯酶。纯化后的酶的相对分子质量为31000，含有天冬酰胺连接的寡糖。该酶能从小麦麸中释放出乙酸，当使用芳香酯作为底物时，只水解α-萘乙酸酯和丙酸酯，暂被归类为羧酸酯酶（EC 3.1.1.1）。克隆并测定了编码乙酰酯酶的基因序列。推导的氨基酸序列表明，乙酰酯酶最初作为一个由304个氨基酸残基组成的前体产生，翻译后转化为一个由275个氨基酸残基组成的成熟蛋白。乙酰酯酶的部分序列与白地霉和柱形假丝酵母脂肪酶活性位点丝氨酸附近的区域相似。存在一个推测的天冬酰胺连接寡糖的独特位点。
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