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. 1991 Jun 1;65(1):9-13.
doi: 10.1016/0378-1097(91)90462-j.

Purification and characterization of a cell wall hydrolase encoded by the cwlA gene of Bacillus subtilis

A Kuroda  1 , M Imazeki, J Sekiguchi
Affiliations

Purification and characterization of a cell wall hydrolase encoded by the cwlA gene of Bacillus subtilis

A Kuroda et al. FEMS Microbiol Lett. .

Abstract

A cell wall hydrolase of Bacillus subtilis was prepared from Escherichia coli cells harboring a plasmid containing the B. subtilis cwlA gene and purified by hydroxyapatite column chromatography and HPLC through TSK-gel G3000SWXL. In contrast to the molecular mass of 29,919 Da deduced from its nucleotide sequence, the purified CWLA is a 23 kDa protein. Characterization of the specific substrate bond cleaved by CWLA indicated the enzyme is an N-acetylmuramyl-L-alanine amidase. A 32-kDa precursor protein was detected on zymography of a crude cell homogenate. Some of the enzymatic properties of CWLA are also described.

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