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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
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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 0300-922X
Full text not available from this repository.Abstract
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 |
| ISSN: | 0300-922X |
| Date: | 7 June 1993 |
| Number: | 11 |
| Number of Pages: | 9 |
| Page Range: | pp. 1225-1233 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/21281 |
Data sourced from Thomson Reuters' Web of Knowledge
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