Characterization of a periplasmic insulin-cleaving metalloproteinase from Acinetobacter calcoaceticus.
In Acinetobacter calcoaceticus, a Gram-negative bacterial species, a soluble insulin-degrading proteinase, located in the periplasm as well as in the cytosol, could be established. The periplasmic and cytosolic enzymes agree in their inhibition pattern, pH-optimum and molecular weight. The insulin-degrading enzyme of Acinetobacter calcoaceticus resembles the corresponding proteinases of Escherichia coli. It is a metalloproteinase with a pH-optimum in the neutral range and can be reactivated by divalent ions after EDTA-inhibition, but it is not entirely identical with any of the described proteinases of Escherichia coli in its inhibitory behaviour.
Fricke
B
B
Institut für Biochemie, Martin-Luther-Universität Halle-Wittenberg, Saale.
Aurich
H
H
D000150:Acinetobacter / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D007328:Insulin / Q000378:metabolism*; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000378:metabolism; D008666:Metalloendopeptidases / Q000378:metabolism*; D009113:Muramidase / Q000494:pharmacology; D017830:Octoxynol; D011092:Polyethylene Glycols; D013347:Subcellular Fractions / Q000201:enzymology
D007328:Insulin; D011092:Polyethylene Glycols; D017830:Octoxynol; D008291:Malate Dehydrogenase; D009113:Muramidase; D008666:Metalloendopeptidases