Purification and partial characterization of a dipeptidyl peptidase from Prevotella intermedia.
A peptidase hydrolyzed X-Pro-p-nitroanilide was purified from the cell extract of Prevotella intermedia ATCC 25611 by ion-exchange chromatography and hydrophobic interaction chromatography. The purified enzyme exhibited a molecular size of 74 kDa from sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the maximum enzyme activity was found between pH 7.0 and pH 7.5. This peptidase was a serine enzyme and hydrolyzed Lys-Pro-p-nitroanilide, Arg-Pro-p-nitroanilide, and Ala-Pro-p-nitroanilide, but Lys-Ala-p-nitroanilide was not split. The enzyme may be classified as a dipeptidyl peptidase IV.
Shibata
Y
Y
Department of Oral Microbiology, Matsumoto Dental University, Shiojiri, Japan.
Miwa
Y
Y
Hirai
K
K
Fujimura
S
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D018819:Dipeptidyl Peptidase 4 / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D018713:Prevotella intermedia / Q000201:enzymology* / Q000302:isolation & purification; D037521:Virulence Factors
D001426:Bacterial Proteins; D037521:Virulence Factors; D018819:Dipeptidyl Peptidase 4