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A new biocatalyst in peptide chemistry: the BL-GSE
Valérie Rolland, René Lazaro, Philippe Viallefont

A new biocatalyst in peptide chemistry: the BL-GSE

Science & Mathematics Published 1994 Verification Pending

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.

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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 »