Takegawa K, Mikami B, Iwahara S, Morita Y, Yamamoto K, Tochikura T
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
Eur J Biochem. 1991 Nov 15;202(1):175-80. doi: 10.1111/j.1432-1033.1991.tb16359.x.
The complete amino acid sequence of endo-beta-N-acetylglucosaminidase from Flavobacterium sp. has been determined by analysis of peptides after cleavage with lysyl endopeptidase, pepsin and chymotrypsin. The protein consists of a single polypeptide chain consisting of 267 amino acid residues and a molecular mass of 27972 Da. The sequence of Flavobacterium endo-beta-N-acetylglucosaminidase is very close to that of the Streptomyces enzyme (endo-H), having 60% similarity and very similar hydropathy profiles. Similarities were also found between Flavobacterium endo-beta-N-acetylglucosaminidase and chitinases from Bacillus circulans, Serratia marcescens and Phaseolus vulgaris.
通过对经赖氨酰内肽酶、胃蛋白酶和胰凝乳蛋白酶切割后的肽段进行分析，确定了来自黄杆菌属（Flavobacterium sp.）的内切-β-N-乙酰氨基葡糖苷酶的完整氨基酸序列。该蛋白质由一条由267个氨基酸残基组成的单多肽链构成，分子量为27972道尔顿。黄杆菌内切-β-N-乙酰氨基葡糖苷酶的序列与链霉菌酶（内切-H）的序列非常接近，相似度为60%，且亲水性图谱非常相似。在黄杆菌内切-β-N-乙酰氨基葡糖苷酶与环状芽孢杆菌、粘质沙雷氏菌和菜豆的几丁质酶之间也发现了相似性。
