Purification and characterization of alkaline phosphatase containing phosphotyrosyl phosphatase activity from the bacterium Prevotella intermedia

被引：21

作者：

Ansai, T ^{[1
]}

Awano, S ^{[1
]}

Chen, XC ^{[1
]}

Fuchi, T ^{[1
]}

Arimoto, T ^{[1
]}

Akifusa, S ^{[1
]}

Takehara, T ^{[1
]}

机构：

[1] Kyushu Dent Coll, Dept Prevent Dent, Kokurakita Ku, Kitakyushu, Fukuoka 8028580, Japan

来源：

FEBS LETTERS | 1998年 / 428卷 / 03期

关键词：

alkaline phosphatase; thermostable; phosphotyrosyl phosphatase; Prevotella intermedia;

D O I：

10.1016/S0014-5793(98)00514-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 mas highly stable even at 80 degrees C. It exhibited substantial activity against tyrosine-phosphate-containing Raytide. The phosphatase activity was sensitive to orthovanadate and Zn2+ 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. (C) 1998 Federation of European Biochemical Societies.

引用

页码：157 / 160

页数：4

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