Abstract
The neutral proteases are a group of metallo endopeptidases primarily of microbial origin which have a similar substrate specificity and have neutral pH activity optima. These enzymes have been isolated fromBacilli, Streptomyces, Aspergilli,andPseudomonas among others.1 All of these enzymes catalyze the hydrolysis of peptide bonds of which the imino group is contributed by a hydrophobic amino acid, particularly leucine and phenylalanine. The neutral proteases isolated fromB. subtilis,2 B. megaterium,3 -5 B. cereus 6,7andB. thermoproteolyticus 8,9,10contain a single zinc atom and are stabilized by calcium and other divalent cations. These enzymes generally lack cysteine in their structures and Pangburnet a1.11recently reported similarity in sequences of theB. subtilis neutral protease and thermolysin. In spite of the great similarity in catalytic and structural properties these enzymes differ markedly in thermal stability
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Feder, J., Aufderheide, N., Wildi, B.S. (1976). Studies on The Inhibition of Thermolysin. In: Zuber, H. (eds) Enzymes and Proteins from Thermophilic Microorganisms Structure and Function. Experientia Supplementum, vol 26. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7675-9_3
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DOI: https://doi.org/10.1007/978-3-0348-7675-9_3
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