Potencies of phosphine peptide inhibitors of mammalian thimet oligopeptidase and neurolysin on two bacterial pz peptidases.
Pz peptidases A and B, from a thermophile Geobacillus collagenovorans MO-1, 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.
Sugihara
Yusuke
Y
Department of Applied Biochemistry, Kyoto Prefectural University, Sakyo, Kyoto, Japan.
Kawasaki
Akio
A
Tsujimoto
Yoshiyuki
Y
Matsui
Hiroshi
H
Watanabe
Kunihiko
K
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000378:metabolism*; D008970:Molecular Weight; D010720:Phosphines / Q000494:pharmacology*; D010957:Plasmids / Q000235:genetics; D011401:Promoter Regions, Genetic / Q000235:genetics; D011480:Protease Inhibitors / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D010720:Phosphines; D011480:Protease Inhibitors; D011994:Recombinant Proteins; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase; C062316:neurolysin