Peptide synthesis by proteases in organic solvents: medium effect on substrate specificity.

Abstract:

:The substrate specificities of alpha-chymotrypsin and subtilisins for peptide synthesis in hydrophilic organic solvents were investigated. Chymotrypsin exhibited high specificity to aromatic amino acids as acyl donors, while subtilisin Carlsberg and subtilisin BPN' were specific to aromatic and neutral aliphatic amino acids, in accordance with the S1 specificities of the enzymes for peptide hydrolysis in aqueous solutions. On the contrary, chymotrypsin exhibited higher specificities to hydrophilic amino acid amides as acyl acceptors (nucleophiles) for peptide synthesis with N-acetyl-L-tyrosine ethyl ester, in contrast to the S1' specificity for peptide hydrolysis and peptide synthesis in aqueous solutions. Furthermore, nucleophile specificity changed with the change in water-organic solvent composition; the increase in water content led to increase in relative reactivity of leucinamide to that of alaninamide. It was also found that protection of the carboxyl group of alanine by amidation is much preferable to protection by esterification in terms of reactivity as nucleophiles.

journal_name

Enzyme Microb Technol

authors

Nagashima T,Watanabe A,Kise H

doi

10.1016/0141-0229(92)90102-t

keywords:

subject

Has Abstract

pub_date

1992-10-01 00:00:00

pages

842-7

issue

10

eissn

0141-0229

issn

1879-0909

pii

0141-0229(92)90102-T

journal_volume

14

pub_type

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