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Studies on peptide amidase‐catalysed C‐terminal peptide amidation in organic media with respect to its substrate specificity
Author(s) -
Čeřovský Václav,
Kula MariaRegina
Publication year - 2001
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.2001.tb00925.x
Subject(s) - chemistry , amidase , amide , peptide , substrate (aquarium) , hydrolysis , dimethylformamide , peptide bond , stereochemistry , organic chemistry , biochemistry , oceanography , solvent , geology
Peptide amidase‐catalysed amidations of the C‐ terminal carboxylic group of peptides were studied using model substrates of a large series of N α ‐protected di‐, tri‐, tetra‐ and penta‐peptides in the presence of NH 4 HCO 3 as the ammonium source. The maximal yields of amide syntheses were achieved in a medium consisting of acetonitrile with 20–25 vol% of dimethylformamide and 3 vol% of water. Under these conditions, the substrate specificity of the enzyme was more restricted in the synthetic reaction than was found for the amide hydrolysis. Elongation of the peptide chain had a negative effect on enzymic amidation. Thus the direct amidation of N α ‐t‐butoxycarbonyl‐protected Leu‐enkephalin resulted in a low yield of protected enkephalin amide.