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protealysin propeptide domain-containing protein
This propeptide is cleaved during maturation of protealysin [1-2]. Before cleavage it interacts with the catalytic domain, blocking the active site [3]. [1]. 16442309. Cloning, sequencing, expression, and characterization of protealysin, a novel neutral proteinase from Serratia proteamaculans representing a new group of thermolysin-like proteases with short N-terminal region of precursor. Demidyuk IV, Kalashnikov AE, Gromova TY, Gasanov EV, Safina DR, Zabolotskaya MV, Rudenskaya GN, Kostrov SV;. Protein Expr Purif. 2006;47:551-561. [2]. 19324072. Processing of protealysin precursor. Gromova TY, Demidyuk IV, Kozlovskiy VI, Kuranova IP, Kostrov SV;. Biochimie. 2009;91:639-645. [3]. 19915005. Crystal structure of the protealysin precursor: insights into propeptide function. Demidyuk IV, Gromova TY, Polyakov KM, Melik-Adamyan WR, Kuranova IP, Kostrov SV;. J Biol Chem. 2010;285:2003-2013. (from Pfam)
Thermolysin metallopeptidase, catalytic domain
M4 family metallopeptidase
M4 family metalopeptidase is a zinc metallopeptidase that contains an HEXXH motif, where the histidines are zinc ligands and the glutamate is an active site residue, preferably cleaving Xaa+Yaa, in which Xaa is a hydrophobic residue and Yaa is Leu, Phe, Ile, or Val
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