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- W148446504 abstract "Publisher Summary This chapter reviews activity, specificity and structural chemistry of Listeria metalloprotease Mpl. Listena monocytogenes is a gram-positive nonspore-forming, facultative intracellular rod-shaped bacterium which is capable of causing serious infections in human and animals. L. monocytogenes Mpl protease contains 510 amino acids with a predicted molecular mass of 57.4 kDa. Following cleavage of the N-terminal 24 amino acid signal sequence, the 55 kDa inactive zymogen is secreted to the external medium. Mature active protease has a molecular mass of 36 kDa as a result of further processing of the N-terminal 180 amino acids. The calculated pi of Mpl is 6.64. Mpl is the most heat-stable natural thermolysin protease. The genetic and biochemical evidence available suggests that Mpl is a neutral protease of the thermolysin family. An unusual feature of Mpl is the presence of several cysteine residues that could create disulfide bridges to stabilize the enzyme. None of the known natural thermolysin-like proteases is known to contain disulfide bridges. A threedimensional model built on the homology with thermolysin that accounts for the extreme salt, pH and temperature requirements of this enzyme has been described." @default.
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- W148446504 date "2004-01-01" @default.
- W148446504 modified "2023-10-16" @default.
- W148446504 title "Listeria metalloprotease Mpl" @default.
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- W148446504 doi "https://doi.org/10.1016/b978-0-12-079611-3.50105-1" @default.
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