Kinetic and site-directed mutagenesis studies of prevotella intermedia acid phosphatase.
Site-directed mutagenesis was used to examine the roles of the conserved histidine, arginine and cysteine residues in acid phosphatase from Prevotella intermedia (PiACP). The replacement of histidine and arginine residues resulted in the elimination of the PiACP activity while the cysteine mutants retained activity. These results suggest that the histidine and arginine residues are essential for catalysis.
Chen
Xiaochi
X
Department of Preventive Dentistry, Kyushu Dental College, Kitakyushu 803-85802 Japan.
Ansai
Toshihiro
T
Barik
Sailen
S
Takehara
Tadamichi
T
D000135:Acid Phosphatase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D019943:Amino Acid Substitution; D001120:Arginine / Q000235:genetics / Q000378:metabolism; D002384:Catalysis; D017931:DNA Primers / Q000235:genetics; D006639:Histidine / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism; D018713:Prevotella intermedia / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D017931:DNA Primers; D011994:Recombinant Proteins; D019000:Phosphotyrosine; D006639:Histidine; D001120:Arginine; D000135:Acid Phosphatase