Overexpression, purification, and characterization of Bacillus subtilis N-acetylmuramoyl-L-alanine amidase CwlC.
N-acetylmuramoyl-L-alanine amidase CwlC of Bacillus subtilis was overproduced in Escherichia coli and purified 21-fold. The amidase hydrolyzed type A cell walls such as B. subtilis. The amidase bound slightly to the Microbacterium lacticum cell wall (type B), but did not entirely hydrolyze it. The presence of calcium or magnesium ion increased the resistance of the amidase to heat denaturation.
Shida
T
T
Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda, Nagano, Japan.
Hattori
H
H
Ise
F
F
Sekiguchi
J
J
D000818:Animals; D001173:Arthrobacter / Q000378:metabolism; D001407:Bacillus / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002473:Cell Wall / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D016982:Micrococcus luteus / Q000378:metabolism; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000378:metabolism; D013696:Temperature
D001426:Bacterial Proteins; C083494:cwlC protein, Bacillus subtilis; D009238:N-Acetylmuramoyl-L-alanine Amidase; D002118:Calcium