Lei S P, Lin H C, Wang S S, Callaway J, Wilcox G
J Bacteriol. 1987 Sep;169(9):4379-83. doi: 10.1128/jb.169.9.4379-4383.1987.
The pelB gene encodes pectate lyase B, one of three pectate lyases identified in Erwinia carotovora EC. Pectate lyase B was purified from Escherichia coli containing the pelB gene on a recombinant plasmid. The activity of the protein was optimal at a pH of 8.3. The amino acid composition, N-terminal amino acid sequence, and C-terminal peptide sequence were determined and compared with the polypeptide sequence deduced from the DNA sequence of pelB. Purified pectate lyase B started at amino acid 23 of the predicted sequence, suggesting that a 22-amino-acid leader peptide had been removed. Pectate lyase B of E. carotovora EC and pectate lyase B of E. chrysanthemi EC16 contain 352 and 353 amino acids, respectively (N. T. Keen, S. Tanaki, W. Belser, D. Dahlbeck, and B. Staskawicz, J. Bacteriol. 168:595-606, 1986). The two proteins are 72% homologous on the basis of DNA sequence data, and 75% of the amino acids are identical.
pelB基因编码果胶酸裂解酶B，它是在胡萝卜软腐欧文氏菌EC中鉴定出的三种果胶酸裂解酶之一。果胶酸裂解酶B是从含有重组质粒上pelB基因的大肠杆菌中纯化得到的。该蛋白的活性在pH 8.3时最佳。测定了其氨基酸组成、N端氨基酸序列和C端肽序列，并与从pelB的DNA序列推导的多肽序列进行了比较。纯化的果胶酸裂解酶B从预测序列的第23个氨基酸开始，这表明一个22个氨基酸的前导肽已被去除。胡萝卜软腐欧文氏菌EC中的果胶酸裂解酶B和菊苣欧文氏菌EC16中的果胶酸裂解酶B分别含有352和353个氨基酸（N.T.基恩、S.田木、W.贝尔瑟、D.达尔贝克和B.斯塔斯卡维茨，《细菌学杂志》168:595 - 606，1986年）。根据DNA序列数据，这两种蛋白的同源性为72%，75%的氨基酸相同。
