| Literature DB >> 3040692 |
S P Lei, H C Lin, S S Wang, J Callaway, G Wilcox.
Abstract
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.Entities:
Mesh：
Substances：
Year: 1987 PMID： 3040692 PMCID： PMC213756 DOI： 10.1128/jb.169.9.4379-4383.1987
Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490