Substrate specificity of α-chymotrypsin-catalyzed esterification in organic media
(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.
(Less)
- author
- Clapés, Pere and Adlercreutz, Patrick LU
- organization
- publishing date
- 1991-12-11
- 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}}, }