The role of membrane-promoted multi-point hydrophobic interactions between peptide catalysts and enantiomeric substrates in highly stereoselective hydrolyses of amino acid esters-Reference-Cited by-同舟云学术

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The role of membrane-promoted multi-point hydrophobic interactions between peptide catalysts and enantiomeric substrates in highly stereoselective hydrolyses of amino acid esters

Published:1996-07 Issue:1 Volume:110 Page:L1-L4
ISSN:1381-1169
Container-title:Journal of Molecular Catalysis A: Chemical
language:en
Short-container-title:Journal of Molecular Catalysis A: Chemical

Author:

Ohkubo Katsutoshi,Urabe Kenji,Yamamoto Junji,Usui Satoshi,Sagawa Takashi

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,Process Chemistry and Technology,Catalysis

Reference6 articles.

1. Efficient stereoselective hydrolysis of enantiomeric amino acid esters by bilayer vesicular systems which include di- or tri-peptide histidine catalysts

2. Highly efficient enantioselective hydrolysis of short chain N-acetyl amino acid p-nitrophenyl esters catalysed by esterase models

3. Membrane matrix for the hydrolysis of amino acid esters with marked enantioselectivity

4. Kinetics and molecular modelling studies on the stereoselective hydrolysis of enantiomeric esters by dipeptide catalysts

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