A new metalloproteinase from Pseudomonas fluorescens biotype I.
Isolation and purification of a metalloproteinase from Pseudomonas fluorescens Biotype I are described. The molecular mass of the enzyme is 46 kDa, its isoelectric point is 8.1, its activity is trypsin-like. The amino-acid composition of the single chain protein is given. One molecule of the enzyme contains 1 atom of zinc and 9 atoms of calcium.
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D005285:Fermentation; D007525:Isoelectric Focusing; D008666:Metalloendopeptidases; D008670:Metals / Q000032:analysis; D008970:Molecular Weight; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D013379:Substrate Specificity
D008670:Metals; D010450:Endopeptidases; D008666:Metalloendopeptidases