SELECTIVITY AND SPECIFICITY IN SUBSTRATE-BINDING TO PROTEASES - NOVEL HYDROLYTIC REACTIONS CATALYZED BY ALPHA-CHYMOTRYPSIN SUSPENDED IN ORGANIC-SOLVENTS WITH LOW WATER-CONTENT AND MEDIATED BY AMMONIUM HYDROGEN CARBONATE
UNSPECIFIED (1993) SELECTIVITY AND SPECIFICITY IN SUBSTRATE-BINDING TO PROTEASES - NOVEL HYDROLYTIC REACTIONS CATALYZED BY ALPHA-CHYMOTRYPSIN SUSPENDED IN ORGANIC-SOLVENTS WITH LOW WATER-CONTENT AND MEDIATED BY AMMONIUM HYDROGEN CARBONATE. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1 (11). pp. 1225-1233. ISSN 0300-922XFull text not available from this repository.
Alpha-chymotrypsin suspended in organic solvents with low water content catalysed hydrolytic reactions in the presence of ammonium hydrogen carbonate. Molecular modelling studies were carried out and structure-reactivity relationships were established by studying the hydrolysis of amino acid derivatives and analogues. The enzyme was found to be stereoselective with respect to the hydrolysis of L-amino acid derivatives, but no stereoselectivity was observed when alpha-hydroxy esters were used as substrates. A general procedure for the resolution of aromatic amino acid esters is given. The results are interpreted in terms of molecular modelling based on X-ray crystallographic data and literature data.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1|
|Publisher:||ROYAL SOC CHEMISTRY|
|Date:||7 June 1993|
|Number of Pages:||9|
|Page Range:||pp. 1225-1233|
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