A new biocatalyst in peptide chemistry: the BL-GSE
Overview & Synopsis
Protease mediated bond synthesis, first reported by Bergmann and Fraenkel-Conrat [1], has received increasing interest due to the inherent advantages it possesses over chemically-based peptide bond syntheses. A Glu/Asp specific endoprotease, very recently isolated from Bacillus licheniformis[2], belonging to the serin group and called BL-GSE, is able to catalyse the coupling of a lot of different nucleophiles (H-Xxx-NH2) corresponding to P1' position (Schechter and Berger notation) on Glu or Asp residues under kinetic control [3]. The effect of water miscible organic solvents (DMF,Methanol or acetonitrile) has been studied in an attempt to diminish esterase activity and secondary reverse hydrolysis of the new peptide bond.
hal.science)
← / → for pages • + / - for zoom • 0 to fit width
Powered by Mozilla PDF.js v3.11
Document Information
| Document Title | A new biocatalyst in peptide chemistry: the BL-GSE |
|---|---|
| Author / Organization | Valérie Rolland, René Lazaro, Philippe Viallefont |
| Subject & Discipline | Multidisciplinary Academic Open Research |
| Categories | Science & Mathematics |
| Publication Year | 1994 |
| License / Rights | Open Access / Creative Commons |
| Resource Verification | Listed PDF (Verification Pending) |
| Original Host Website |
HAL Open Science
(hal.science)
|
| File Format | application/pdf (Portable Document Format) |
| Language | EN |
| Catalog ID | DOC-111072 |
| Original Source Link | Visit Source Page on hal.science » |