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CelS: a novel endoglucanase identified from Erwinia carotovora subsp. carotovora.

作者信息

Saarilahti H T, Henrissat B, Palva E T

机构信息

Department of Molecular Genetics, Swedish University of Agricultural Sciences, Uppsala.

出版信息

Gene. 1990 May 31;90(1):9-14. doi: 10.1016/0378-1119(90)90433-r.

DOI:10.1016/0378-1119(90)90433-r
PMID:2379837
Abstract

A plasmid clone expressing a beta(1,4)-glucan glucanohydrolase (EC 3.2.1.4; endoglucanase) in Escherichia coli was isolated from a genomic library of Erwinia carotovora subsp. carotovora. The DNA segment carrying the corresponding structural gene, named celS, contained an open reading frame encoding a 264-amino acid (aa) polypeptide. The N-terminal aa sequence of CelS showed that the protein was synthesized with a 32-aa cleavable signal peptide. The mature 232-aa CelS had a calculated Mr of 26,228 and pI of 5.5. The pH optimum was about 6.8 and the temperature optimum was between 45 and 55 degrees C. Comparison of the aa sequence of CelS by hydrophobic cluster analysis with a range of cellulases and other quasi-isofunctional enzymes revealed only very limited sequence similarities, suggesting that the CelS protein may represent the first member of an additional cellulase family.

摘要

相似文献

1
CelS: a novel endoglucanase identified from Erwinia carotovora subsp. carotovora.
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2
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