Potencies of phosphine peptide inhibitors of mammalian thimet oligopeptidase and neurolysin on two bacterial Pz peptidases

被引:6
|
作者
Sugihara, Yusuke [1 ]
Kawasaki, Akio [1 ]
Tsujimoto, Yoshiyuki [1 ]
Matsui, Hiroshi [1 ]
Watanage, Kunihiko [1 ]
机构
[1] Kyoto Prefectural Univ, Dept Appl Biochem, Kyoto 6068522, Japan
关键词
Pz-peptidase; thimet oligopeptidase; neurolysin; phosphine peptide; oligopeptidase;
D O I
10.1271/bbb.60534
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
Pz peptidases A and bacillus collagenovorans B, from a thermophile Geo-bacillus recognize collagen-specific tripeptide units (Gly-Pro-Xaa). They share similarities in function but extremely low identities in primary sequence with mammalian thimet oligopeptidase (TOP) and neurolysin. Three phosphine peptide inhibitors that selectively inhibit TOP and neurolysin on two bacterial Pz peptidases were investigated. They showed potent inhibition of both Pz peptidases in a range from 10 to 100 nm.
引用
收藏
页码:594 / 597
页数:4
相关论文
共 3 条
  • [1] Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin
    Oliveira, V
    Campos, M
    Melo, RL
    Ferro, ES
    Camargo, ACM
    Juliano, MA
    Juliano, L
    BIOCHEMISTRY, 2001, 40 (14) : 4417 - 4425
  • [2] Two thimet oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile, Geobacillus collagenovorans MO-1
    Miyake, R
    Shigeri, Y
    Tatsu, Y
    Yumoto, N
    Umekawa, M
    Tsujimoto, Y
    Matsui, H
    Watanabe, K
    JOURNAL OF BACTERIOLOGY, 2005, 187 (12) : 4140 - 4148
  • [3] The Exquisite Structure and Reaction Mechanism of Bacterial Pz-peptidase A toward Collagenous Peptides X-RAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS OF PZ-PEPTIDASE A REVEALS DIFFERENCES FROM MAMMALIAN THIMET OLIGOPEPTIDASE
    Kawasaki, Akio
    Nakano, Hiroaki
    Hosokawa, Allin
    Nakatsu, Toru
    Kato, Hiroaki
    Watanabe, Kunihiko
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (45) : 34972 - 34980