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

9Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

Sugihara, Y., Kawasaki, A., Tsujimoto, Y., Matsui, H., & Watanabe, K. (2007). Potencies of phosphine peptide inhibitors of mammalian thimet oligopeptidase and neurolysin on two bacterial Pz peptidases. Bioscience, Biotechnology and Biochemistry, 71(2), 594–597. https://doi.org/10.1271/bbb.60534

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free