title: Three different types of catalases in Klebsiella pneumoniae.
abstract: Crude extracts from aerobically grown bacterium Klebsiella pneumoniae contain three different types of catalases, designated KpT, KpCP, and KpA, whose activities in crude extracts are in the ratio 4.1:1:0.3. KpT resembles typical catalases: its molecular weight is 259,000, its activity is independent of pH in the range 5.5-10.5, it is stable at 52 degrees C but loses 80% of its activity when incubated at 60 degrees C for 45 min, and it has hydrophobic properties revealed by binding to phenyl-Sepharose and stability in ethanol-chloroform. KpCP is a catalase-peroxidase with a molecular weight of 278,000, has a sharp pH optimum at 6.3, and is inactivated by treatment at 52 degrees C for 45 min and by ethanol-chloroform. KpA has been reported to be a dimer with molecular weight of 160,000 which contains a chlorin-type heme, has a plateau of maximal activity between pH's 2.8 and 11.8, and is stable to treatment with ethanol-chloroform and to incubation at 70 degrees C. All three enzymes are inhibited by cyanide.
authors.affiliation: Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel.
authors.forename: I
authors.initials: I
authors.lastname: Goldberg
authors.forename: A
authors.initials: A
authors.lastname: Hochman
mesh_terms: D002374:Catalase / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D008970:Molecular Weight; D013816:Thermodynamics
chemical_list: D007527:Isoenzymes; D002374:Catalase