17528-17-5Relevant academic research and scientific papers
Chloride-Assisted Peptide Macrocyclization
Cindro, Nikola,Horvat, Gordan,Rinkovec, Tamara,Riva, Davide,Speranza, Giovanna,Tomi?i?, Vladislav,Vidovi?, Nikolina
supporting information, (2020/03/26)
The role of the Cl- anion as a templating agent for the synthesis of cyclopeptides was assessed through the preparation of three new homocyclolysines and other six cyclic peptides by head-to-tail lactamization. Isolated yields of products obtai
Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins
Usuki, Hirokazu,Yamamoto, Yukihiro,Arima, Jiro,Iwabuchi, Masaki,Miyoshi, Shozo,Nitoda, Teruhiko,Hatanaka, Tadashi
supporting information; experimental part, p. 2327 - 2335 (2011/05/02)
A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.
Engineered transaminopeptidase, aminolysin-S for catalysis of peptide bond formation to give linear and cyclic dipeptides by one-pot reaction
Usuki, Hirokazu,Uesugi, Yoshiko,Arima, Jiro,Yamamoto, Yukihiro,Iwabuchi, Masaki,Hatanaka, Tadashi
supporting information; experimental part, p. 580 - 582 (2010/05/01)
Aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 was engineered into transaminopeptidase and used to catalyze an aminolysis reaction to give linear and cyclic dipeptides from cost-effective substrates such as the ester derivatives of amino
Retro Aza Diels-Alder Reactions of 2-Azanorbornenes: Improved Methods for the Unmasking of Primary Amines
Grieco, Paul A.,Clark, Jerry D.
, p. 2271 - 2272 (2007/10/02)
The unmasking of primary amines via the heterocycloreversion of N-alkyl-2-azanorbornenes can be catalyzed by either copper(II) or a sulfonic acid based ion exchange resin which obviates the necessity of employing a reactive dienophile to trap the cyclopentadiene as it is produced.
