Okazaki Katsuichiro, Nishimura Naohito, Matsuoka Fumiyoshi, Hayakawa Shigeru
Department of Applied Biological Science, Faculty of Agriculture, Kagawa University Japan.
Biosci Biotechnol Biochem. 2007 Jun;71(6):1568-71. doi: 10.1271/bbb.70030.
The gluA gene, encoding an endo-beta-1,3-glucanase from Arthrobacter sp. (strain NHB-10), was cloned and analyzed. The deduced endo-beta-1,3-glucanase amino acid sequence was 750 amino acids long and contained a 42 amino acid signal peptide with a mature protein of 708 amino acids. There was no similarity to known endo-beta-1,3-glucanases, but GluA was partially similar to two fungal exo-beta-1,3-glucanases in glycoside hydrolase (GH) family 55. Of five possible residues for catalysis and two motifs in two beta-helix heads of GH family 55, three residues and one motif were conserved in GluA, suggesting that GluA is the first bacterial endo-beta-1,3-glucanase in GH family 55. Significant similarity was also found to two proteins of unknown function from Streptomyces coelicolor A3(2) and S. avermitilis.
克隆并分析了来自节杆菌属（菌株NHB - 10）的编码内切β-1,3-葡聚糖酶的gluA基因。推导的内切β-1,3-葡聚糖酶氨基酸序列长750个氨基酸，包含一个42个氨基酸的信号肽，成熟蛋白为708个氨基酸。它与已知的内切β-1,3-葡聚糖酶没有相似性，但GluA与糖苷水解酶（GH）家族55中的两种真菌外切β-1,3-葡聚糖酶部分相似。在GH家族55的两个β-螺旋头部的五个可能的催化残基和两个基序中，GluA中有三个残基和一个基序是保守的，这表明GluA是GH家族55中的第一个细菌内切β-1,3-葡聚糖酶。还发现它与天蓝色链霉菌A3(2)和阿维链霉菌中两个功能未知的蛋白质有显著相似性。
