Amine catalysis in the vinylic substitution of α-methylthio-α-arylmethylene Meldrum's acids and its absence in the substitution of methyl β-iodo-α-nitrocinnamate by amines

Author(s):  
Michal Beit-Yannai ◽  
Xin Chen ◽  
Zvi Rappoport
2018 ◽  
Vol 15 (10) ◽  
pp. 883-890
Author(s):  
Ewelina Najda-Mocarska ◽  
Anna Zakaszewska ◽  
Karolina Janikowska ◽  
Slawomir Makowiec
Keyword(s):  

2016 ◽  
Vol 81 (6) ◽  
pp. 2420-2431 ◽  
Author(s):  
G. Madhusudhan Reddy ◽  
Chi-Ting Ko ◽  
Kai-Hong Hsieh ◽  
Chia-Jui Lee ◽  
Utpal Das ◽  
...  

ChemInform ◽  
2014 ◽  
Vol 45 (37) ◽  
pp. no-no
Author(s):  
Simon Krautwald ◽  
Michael A. Schafroth ◽  
David Sarlah ◽  
Erick M. Carreira
Keyword(s):  

2021 ◽  
Author(s):  
Thomas Williams ◽  
Yu-Hsuan Tsai ◽  
Louis Luk

Abstract Here, incorporation of secondary amine by genetic code expansion was used to expand the potential protein templates for artificial enzyme design. Pyrrolysine analogue containing a D-proline could be stably incorporated into proteins, including the multidrug-binding LmrR and nucleotide-binding dihydrofolate reductase (DHFR). Both modified scaffolds were catalytically active, mediating transfer hydrogenation with a relaxed substrate scope. The protein templates played a distinctive role in that, while the LmrR variants were confined to the biomimetic BNAH as the hydride source, the optimal DHFR variant favorably used the pro-R hydride from NADPH for reactions. Due to the cofactor compatibility, the DHFR secondary amine catalysis could also be coupled to an enzymatic recycling scheme. This work has illustrated the unique advantages of using proteins as hosts, and thus the presented concept is expected to find uses in enabling tailored secondary amine catalysis.


2017 ◽  
Vol 56 (41) ◽  
pp. 12697-12701 ◽  
Author(s):  
Jun Dai ◽  
Dan Xiong ◽  
Tengrui Yuan ◽  
Juan Liu ◽  
Tao Chen ◽  
...  

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