New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme.
New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme.
复制标题
由变青链霉菌产生的新型 α-L-阿拉伯呋喃糖苷酶：abfB 基因的克隆和 DNA 序列以及酶的表征。
DOI：
10.1042/bj3220845
复制
发表时间：
1997
影响因子：
4.1
通讯作者：
D. Kluepfel
中科院分区：
文献类型：
--
作者：
P. Vincent;F. Shareck;C. Dupont;R. Morosoli;D. Kluepfel
从变铅青链霉菌的同源表达系统中克隆了一个完全分泌的α-l-阿拉伯呋喃糖苷酶。该基因位于前面描述的木聚糖酶A基因的上游，进行测序。它是从xlnA基因分化转录的，两个基因被391 nt的顺反子间区域分开，该区域含有富含AT的回文序列。推导的蛋白质的氨基酸序列表明，该酶含有一个独特的催化结构域，它是连接到一个特定的木聚糖结合结构域的连接区。该酶对禾本科木聚糖具有特异的阿拉伯呋喃糖脱支活性，与S. Lividans木聚糖酶并特异性结合木聚糖。从小的阿拉伯木糖苷，它释放阿拉伯糖，经过长时间的温育，纯化的酶也表现出一定的木聚糖分解活性。
A fully secreted alpha-l-arabinofuranosidase was cloned from the homologous expression system of Streptomyces lividans. The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by an intercistronic region of 391nt which contains a palindromic AT-rich sequence. The deduced amino acid sequence of the protein shows that the enzyme contains a distinct catalytic domain which is linked to a specific xylan-binding domain by a linker region. The purified enzyme has a specific arabinofuranose-debranching activity on xylan from Gramineae, acts synergistically with the S. lividans xylanases and binds specifically to xylan. From small arabinoxylo-oligosides, it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well.