scholarly journals Trypsin-Catalyzed Peptide Synthesis with Various p-Guanidinophenyl Esters as Acyl Donors.

1996 ◽  
Vol 44 (8) ◽  
pp. 1585-1587 ◽  
Author(s):  
Haruo SEKIZAKI ◽  
Kunihiko ITOH ◽  
Eiko TOYOTA ◽  
Kazutaka TANIZAWA
2005 ◽  
Vol 27 (16) ◽  
pp. 1199-1203 ◽  
Author(s):  
Sayed Mohiuddin Abdus Salam ◽  
Ken-ichi Kagawa ◽  
Katsuhiro Kawashiro

1984 ◽  
Vol 220 (2) ◽  
pp. 405-416 ◽  
Author(s):  
W Kullmann

The proteinase-catalysed synthesis of [Leu]enkephalin and [Met]enkephalin was studied kinetically. N alpha-t-Butoxycarbonyl-amino acids and peptides or their ethyl esters served as acyl donors, and amino acid phenylhydrazides were used as acyl acceptors. Initial-velocity measurements of alpha-chymotrypsin-catalysed peptide synthesis gave rise to kinetic patterns that are compatible with a ping-pong mechanism modified by a hydrolytic branch. Initial-rate and alternative-substrate inhibition patterns for papain-controlled peptide-bond formation are consistent with a sequential ordered mechanism with the acyl donor as the obligatory first substrate. On the basis of the observed kinetic features, reaction mechanisms are proposed for chymotrypsin- and papain-catalysed peptide synthesis that inversely equal those describing the pathways of proteolysis. The respective initial-velocity expressions for bireactant systems are given, along with the numerical values of the corresponding kinetic parameters.


ChemInform ◽  
2010 ◽  
Vol 24 (39) ◽  
pp. no-no
Author(s):  
K. KAWASHIRO ◽  
K. KAISO ◽  
D. MINATO ◽  
S. SUGIYAMA ◽  
H. HAYASHI

Author(s):  
Toshifumi Miyazawa ◽  
Shin'ichi Nakajo ◽  
Miyako Nishikawa ◽  
Kiwamu Imagawa ◽  
Ryoji Yanagihara ◽  
...  

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