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Substrate specificity of α-chymotrypsin-catalyzed esterification in organic media

Clapés, Pere and Adlercreutz, Patrick LU orcid (1991) In BBA - Protein Structure and Molecular Enzymology 1118(1). p.70-76
Abstract

11 amino acid derivatives were tested as α-chymotrypsin substrates in the esterification reaction with methanol in organic media. The reactions were carried out in water-saturated ethyl acetate and in acetonitrile containing 4% water. α-Chymotrypsin adsorbed on Celite was used as a catalyst. From initial reaction rate measurements, the Michaelis-Menten parameters Vmax and KM were determine. All the amino acid derivatives tested were esterified and the highest values of kcal KM were obtained with the N-acylated aromatic amino acids. Correlations between Michaelis-Menten parameters and physical properties of the substrates such as molar refractivity (MR) and log P were deduced. The results show... (More)

11 amino acid derivatives were tested as α-chymotrypsin substrates in the esterification reaction with methanol in organic media. The reactions were carried out in water-saturated ethyl acetate and in acetonitrile containing 4% water. α-Chymotrypsin adsorbed on Celite was used as a catalyst. From initial reaction rate measurements, the Michaelis-Menten parameters Vmax and KM were determine. All the amino acid derivatives tested were esterified and the highest values of kcal KM were obtained with the N-acylated aromatic amino acids. Correlations between Michaelis-Menten parameters and physical properties of the substrates such as molar refractivity (MR) and log P were deduced. The results show that the specificity of the α-chymotrypsin towards the side chain of the amino acids in organic media is the same as that in aqueous media. However, the specificity towards the N-protecting group is opposite to that in water, so the reaction medium affects the interactions of this part of the molecule with the enzyme to a large extent.

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type
Contribution to journal
publication status
published
subject
keywords
Structure activity relationship, Substrate specificity, α-Chymotrypsin
in
BBA - Protein Structure and Molecular Enzymology
volume
1118
issue
1
pages
7 pages
publisher
Elsevier
external identifiers
  • scopus:0026066828
  • pmid:1764479
ISSN
0167-4838
DOI
10.1016/0167-4838(91)90442-3
language
English
LU publication?
yes
id
1a528a0e-1ab7-4f9e-b70c-f4e7d89894ec
date added to LUP
2019-06-22 18:44:43
date last changed
2024-01-01 12:23:25
@article{1a528a0e-1ab7-4f9e-b70c-f4e7d89894ec,
  abstract     = {{<p>11 amino acid derivatives were tested as α-chymotrypsin substrates in the esterification reaction with methanol in organic media. The reactions were carried out in water-saturated ethyl acetate and in acetonitrile containing 4% water. α-Chymotrypsin adsorbed on Celite was used as a catalyst. From initial reaction rate measurements, the Michaelis-Menten parameters V<sub>max</sub> and K<sub>M</sub> were determine. All the amino acid derivatives tested were esterified and the highest values of k<sub>cal</sub> K<sub>M</sub> were obtained with the N-acylated aromatic amino acids. Correlations between Michaelis-Menten parameters and physical properties of the substrates such as molar refractivity (MR) and log P were deduced. The results show that the specificity of the α-chymotrypsin towards the side chain of the amino acids in organic media is the same as that in aqueous media. However, the specificity towards the N-protecting group is opposite to that in water, so the reaction medium affects the interactions of this part of the molecule with the enzyme to a large extent.</p>}},
  author       = {{Clapés, Pere and Adlercreutz, Patrick}},
  issn         = {{0167-4838}},
  keywords     = {{Structure activity relationship; Substrate specificity; α-Chymotrypsin}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{1}},
  pages        = {{70--76}},
  publisher    = {{Elsevier}},
  series       = {{BBA - Protein Structure and Molecular Enzymology}},
  title        = {{Substrate specificity of α-chymotrypsin-catalyzed esterification in organic media}},
  url          = {{http://dx.doi.org/10.1016/0167-4838(91)90442-3}},
  doi          = {{10.1016/0167-4838(91)90442-3}},
  volume       = {{1118}},
  year         = {{1991}},
}