Isolation and characterization of a microbial Arg/Lys carboxypeptidase, carboxypeptidase F.
Carboxypeptidase F was isolated from a fungal strain F-33 and characterized. The enzyme has the ability to release arginine and lysine from the carboxy terminus of peptides, and showed high specific activity against arginine (140 units mg-1 protein). Optimal temperature and pH for the enzyme reaction were 55 degrees C and pH 8.5, respectively. The enzyme possessed a high thermal stability. Native molecular weight was estimated to be approximately 450,000. Enzymatic activity was inhibited by Co2+, Cd2+, chelating agents and thiol inhibitors.
Matsumura
E
E
Laboratory of Biology, Osaka University of Pharmaceutical Sciences, Japan.
Sato
T
T
Toyoda
N
N
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology; D005658:Fungi / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012988:Soil Microbiology
D002268:Carboxypeptidases