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A bacterial endo-β-1,4-glucuronan lyase, CUL-I from Brevundimonas sp. SH203, belonging to a novel polysaccharide lyase family.
Protein Expression and Purification ( IF 1.4 ) Pub Date : 2019-09-20 , DOI: 10.1016/j.pep.2019.105502
Masako Kikuchi 1 , Naotake Konno 2 , Tomohiro Suzuki 3 , Yuta Fujii 3 , Yutaka Kodama 3 , Akira Isogai 4 , Naoto Habu 5
Affiliation  

Cellouronate is a (1,4)-β-D-glucuronan prepared by TEMPO-mediated oxidation from regenerated cellulose. We have previously isolated a cellouronate-degrading bacterial strain, Brevundimonas sp. SH203, that produces a cellouronate lyase (β-1,4-glucuronan lyase, CUL-I). In this study, the gene encoding CUL-I was cloned, and the recombinant enzyme was heterologously expressed in Escherichia coli. The predicted CUL-I protein is composed of 426 amino acid residues and includes a putative 21-amino acid signal peptide. The recombinant CUL-I specifically depolymerized β-1,4-glycoside linkages of cellouronate, and its mode of action was endo-type, like the native CUL-I. Sequence analysis showed CUL-I has no similarity to previously known polysaccharide lyases (PLs), indicating that CUL-I should be classified into a novel PL family.

中文翻译:

来自Brevundimonas sp。的细菌内切β-1,4-葡糖醛酸聚糖裂解酶CUL-1。SH203,属于新的多糖裂解酶家族。

纤维绒酸酯是通过TEMPO介导的再生纤维素氧化制备的(1,4)-β-D-葡糖醛酸聚糖。我们以前曾分离出可降解纤维素的细菌,即Brevundimonas sp.。SH203,其产生纤维素酸裂合酶(β-1,4-葡糖醛酸聚糖裂合酶,CUL-1)。在该研究中,克隆了编码CUL-1的基因,并且重组酶在大肠杆菌中异源表达。预测的CUL-1蛋白由426个氨基酸残基组成,并包括一个推定的21个氨基酸信号肽。重组CUL-1特异解聚了纤维绒素的β-1,4-糖苷键,其作用方式像天然CUL-1一样是内切型的。序列分析显示CUL-1与先前已知的多糖裂解酶(PL)没有相似性,表明CUL-1应分类为新的PL家族。
更新日期:2019-09-20
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