Active site structure of a hemagglutinating protease from Porphyromonas gingivalis: similarity to clostripain.
The active site of a 44-kDa hemagglutinating arginine-specific protease from the putative periodontopathogen Porphyromonas gingivalis was specifically labeled with N alpha-[3H]acetyllysine chloromethyl ketone. After enzymatic digestion of the labeled enzyme, a labeled active site peptide was isolated by HPLC. The sequence of the active site peptide was determined, after its treatment with NaBH4 to reduce the ketone group of the reagent moiety, to be Asp-Val-Ala-Cys-Val-Asn-Gly. The cysteine residue was found to be the site for labeling. The sequence resembled the active site structure of the arginine-specific cysteine protease clostripain from Clostridium histolyticum.
Nishikata
M
M
Central Research Division, School of Dentistry, Hokkaido University, Sapporo, Japan.
Yoshimura
F
F
D000345:Affinity Labels; D000590:Amino Acid Chloromethyl Ketones / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D006388:Hemagglutinins / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D011480:Protease Inhibitors / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D000345:Affinity Labels; D000590:Amino Acid Chloromethyl Ketones; D006388:Hemagglutinins; C084570:Nalpha-acetyllysine chloromethyl ketone; D011480:Protease Inhibitors; D003546:Cysteine Endopeptidases; C019913:clostripain