Issue 1, 2001
From the journal:

Chemical Communications

Enantioselective hydrolysis of amino acid esters by apomyoglobin: perfect kinetic resolution of a phenylalanine derivative

Katsuhiko Tomisaka,a   Yasuhiro Ishida,a   Katsuaki Konishia  and  Takuzo Aida*a  

* Corresponding authors

a Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
E-mail: aida@macro.t.u-tokyo.ac.jp;
Fax: Fax: +81-3-5841-7310

Abstract

Apoprotein of horse-heart myoglobin promoted enantioselective hydrolysis of 4-nitrophenyl esters of amino acids, which allowed nearly perfect kinetic resolution of racemic N-Boc-phenylalanine ester (Boc-Phe-ONp).

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Article information

DOI
https://doi.org/10.1039/B008403O
Article type
Communication
Submitted
18 Oct 2000
Accepted
20 Nov 2000
First published
18 Dec 2000

Chem. Commun., 2001, 133-134

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Enantioselective hydrolysis of amino acid esters by apomyoglobin: perfect kinetic resolution of a phenylalanine derivative

K. Tomisaka, Y. Ishida, K. Konishi and T. Aida, Chem. Commun., 2001, 133 DOI: 10.1039/B008403O

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