52127-14-7Relevant articles and documents
On the rational design of substrate mimetics: The function of docking approaches for the prediction of protease specificities
Guenther, Robert,Elsner, Christian,Schmidt, Stephanie,Hofmann, Hans-Joerg,Bordusa, Frank
, p. 1442 - 1446 (2004)
The behaviour of substrate mimetics in mediating the acceptance of nonspecific acyl moieties by proteases has been investigated as a direct function of their site-specific ester leaving groups. In this contribution we report on a computational approach to
Electrophotocatalytic C?H Heterofunctionalization of Arenes
Huang, He,Lambert, Tristan H.
supporting information, p. 11163 - 11167 (2021/04/19)
The electrophotocatalytic heterofunctionalization of arenes is described. Using 2,3-dichloro-5,6-dicyanoquinone (DDQ) under a mild electrochemical potential with visible-light irradiation, arenes undergo oxidant-free hydroxylation, alkoxylation, and amination with high chemoselectivity. In addition to batch reactions, an electrophotocatalytic recirculating flow process is demonstrated, enabling the conversion of benzene to phenol on a gram scale.
D-amino acid specific proteases and native all-L-proteins: A convenient combination for semisynthesis
Wehofsky, Nicole,Pech, Andreas,Liebscher, Sandra,Schmidt, Stephanie,Komeda, Hidenobu,Asano, Yasuhisa,Bordusa, Frank
supporting information; experimental part, p. 5456 - 5460 (2009/03/12)
(Figure Presented) Side reactions side-stepped: A D-amino acid specific protease was used for the first time in the chemoenzymatic synthesis of a native protein, the peptidyl prolyl cis/trans isomerase parvulin 10 from E. coli (see scheme). Side reactions that complicate synthesis with L-amino acid specific enzymes are avoided in this approach.
Substrate mimetics-specific peptide ligases: studies on the synthetic utility of a zymogen and zymogen-like enzymes.
Rall, Kathrin,Bordusa, Frank
, p. 9103 - 9106 (2007/10/03)
Although proteases are capable of synthesizing peptide bonds, they are not proficient at peptide fragment ligation. Further manipulations are needed to shift the native enzyme activity from the cleavage to the synthesis of peptides. This account reports on the synthetic potential of nonactivatable trypsinogen and zymogen-like enzymes designed to minimize proteolytic side reactions during peptide synthesis.
Preparation of boc-amino-acid or peptide aldehydes via reduction of corresponding phenyl esters
Zlatoidsky
, p. 150 - 154 (2007/10/02)
A new alternative method for the preparation of amino-acid and peptide aldehydes based on reduction of corresponding phenyl esters with lithium tri(tert-butoxy)aluminium hydride is described.
