Premium
Purification and characterization of alkaline phosphatase containing phosphotyrosyl phosphatase activity from the bacterium Prevotella intermedia
Author(s) -
Ansai Toshihiro,
Awano Shuji,
Chen Xiaochi,
Fuchi Tomoko,
Arimoto Takafumi,
Akifusa Sumio,
Takehara Tadamichi
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00514-6
Subject(s) - prevotella intermedia , alkaline phosphatase , intermedia , phosphatase , bacteria , chemistry , biochemistry , prevotella , microbiology and biotechnology , biology , phosphorylation , enzyme , genetics , porphyromonas gingivalis , art , performance art , art history
A novel alkaline phosphatase, designated PiALP, has been purified and characterized from Prevotella intermedia ATCC 25611, an anaerobe implicated in progressive periodontal disease. The enzyme was a homodimer of apparently identical subunits of M r 54 kDa. Thiol‐reducing agents completely inhibited the purified enzyme. The enzyme was highly stable even at 80°C. It exhibited substantial activity against tyrosine‐phosphate‐containing Raytide. The phosphatase activity was sensitive to orthovanadate and Zn 2+ but highly resistant to okadaic acid. The amino acid sequence of peptides derived from PiALP showed a high degree of identity (65%) with alkaline phosphatases from Zymomonas mobilis and Synechococcus . The present results imply that PiALP might represent a new family of alkaline phosphotyrosyl phosphatases which has not been described previously.