Fluorogenic Peptide Substrate for Quantification of Bacterial Enzyme Activities.

ABSTRACT: A novel peptide substrate (A G G P L G P P G P G G) was developed for quantifying the activities of bacterial enzymes using a highly sensitive Fluorescence Resonance Energy Transfer (FRET) based assay. The peptide substrate was cleaved by collagenase class I, II, Liberase MTF C/T, collagenase NB1, and thermolysin/neutral protease, which was significantly enhanced in the presence of CaCl₂. However, the activities of these enzymes were significantly decreased in the presence of ZnSO₄ or ZnCl₂. Collagenase I, II, Liberase MTF C/T, thermolysin/neutral protease share similar cleavage sites, L^↓G and P^↓G. However, collagenase NB1 cleaves the peptide substrate at G^↓P and P^↓L, in addition to P^↓G. The enzyme acti

SUBMITTER: Al-Abdullah IH 

PROVIDER: S-EPMC5347087 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature