| Literature DB >> 1908396 |
A Kuroda1, M Imazeki, J Sekiguchi.
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.Entities:
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Year: 1991 PMID: 1908396 DOI: 10.1016/0378-1097(91)90462-j
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742