Nucleophile specificity in α-chymotrypsin- and subtilisin-(Bacillus subtilis strain 72) catalyzed reactions
(1992) In BBA - Protein Structure and Molecular Enzymology 1160(2). p.188-192- Abstract
Nucleophilic properties of amino-acids were studied systematically in acyl-transfer reactions catalyzed by α-chymotrypsin and subtilisin from Bacillus subtilis strain 72 (subtilisin 72) using Mal-l-Ala-l-Ala-l-PheOMe as the acyl-group donor. In α-chymotrypsin-catalyzed reactions, the nucleophile reactivities increase in the following order: d-AlaNH2 < GlyNH2 < l-AlaNH2 < l-ScrNH2 < l-ThrNH2 < l-HisNH2 < l-ValNH2 < l-LcuNH2 < l-TrpNH2 < l-MetNH2 < l-NvaNH2 < l-PheNH2 < l-IleNH2 < l-TyrNH2 < l-ArgNH2. In reactions catalyzed by... (More)
Nucleophilic properties of amino-acids were studied systematically in acyl-transfer reactions catalyzed by α-chymotrypsin and subtilisin from Bacillus subtilis strain 72 (subtilisin 72) using Mal-l-Ala-l-Ala-l-PheOMe as the acyl-group donor. In α-chymotrypsin-catalyzed reactions, the nucleophile reactivities increase in the following order: d-AlaNH2 < GlyNH2 < l-AlaNH2 < l-ScrNH2 < l-ThrNH2 < l-HisNH2 < l-ValNH2 < l-LcuNH2 < l-TrpNH2 < l-MetNH2 < l-NvaNH2 < l-PheNH2 < l-IleNH2 < l-TyrNH2 < l-ArgNH2. In reactions catalyzed by subtilisin 72, the reactivities increase as follows: l-LeuNH2 < l- IleNH2 < l-ThrNH2 < l-ArgNH2 < l-TrpNH2 < l-NvaNH2 < l-ValNH2 < l-MctNH2 < l-AlaNH2 < l-ScrNH2 < d-AlaNH2 < GlyNH2. In α-chymotrypsin-catalyzed reactions, hydrophobic interactions are entirely responsible for the differences between the reactivity of the nucleophiles for amides of all the amino-acids tested with the exception of d-AlaNH2, l-ArgNH2 and l-TyrNH2. In the reactions catalyzed by subtilisin 72, Amino-acid side-chain characteristics and the nucleophile reactivities are not related. The data obtained show the low selectivity of the S1′ subsite of subtilisin 72 and high specify of this subsite in α-chymotrypsin.
(Less)
- author
- Gololobov, Mikhail Yu ; Voyushina, Tatyana L. ; Stepanov, Valentin M. and Adlercreutz, Patrick LU
- organization
- publishing date
- 1992-11-20
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Nucleophile specificity, Quantitative structure activity relationship, Substrate specificity, Subtilisin, α-chymotrypsin
- in
- BBA - Protein Structure and Molecular Enzymology
- volume
- 1160
- issue
- 2
- pages
- 5 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:1445945
- scopus:0026442484
- ISSN
- 0167-4838
- DOI
- 10.1016/0167-4838(92)90006-Y
- language
- English
- LU publication?
- yes
- id
- d0b7aa39-cc44-4a3e-9b00-307c20a2096f
- date added to LUP
- 2019-06-22 18:40:48
- date last changed
- 2024-01-01 12:21:33
@article{d0b7aa39-cc44-4a3e-9b00-307c20a2096f, abstract = {{<p>Nucleophilic properties of amino-acids were studied systematically in acyl-transfer reactions catalyzed by α-chymotrypsin and subtilisin from Bacillus subtilis strain 72 (subtilisin 72) using Mal-l-Ala-l-Ala-l-PheOMe as the acyl-group donor. In α-chymotrypsin-catalyzed reactions, the nucleophile reactivities increase in the following order: d-AlaNH<sub>2</sub> < GlyNH<sub>2</sub> < l-AlaNH<sub>2</sub> < l-ScrNH<sub>2</sub> < l-ThrNH<sub>2</sub> < l-HisNH<sub>2</sub> < l-ValNH<sub>2</sub> < l-LcuNH<sub>2</sub> < l-TrpNH<sub>2</sub> < l-MetNH<sub>2</sub> < l-NvaNH<sub>2</sub> < l-PheNH<sub>2</sub> < l-IleNH<sub>2</sub> < l-TyrNH<sub>2</sub> < l-ArgNH<sub>2</sub>. In reactions catalyzed by subtilisin 72, the reactivities increase as follows: l-LeuNH<sub>2</sub> < l- IleNH<sub>2</sub> < l-ThrNH<sub>2</sub> < l-ArgNH<sub>2</sub> < l-TrpNH<sub>2</sub> < l-NvaNH<sub>2</sub> < l-ValNH<sub>2</sub> < l-MctNH<sub>2</sub> < l-AlaNH<sub>2</sub> < l-ScrNH<sub>2</sub> < d-AlaNH<sub>2</sub> < GlyNH<sub>2</sub>. In α-chymotrypsin-catalyzed reactions, hydrophobic interactions are entirely responsible for the differences between the reactivity of the nucleophiles for amides of all the amino-acids tested with the exception of d-AlaNH<sub>2</sub>, l-ArgNH<sub>2</sub> and l-TyrNH<sub>2</sub>. In the reactions catalyzed by subtilisin 72, Amino-acid side-chain characteristics and the nucleophile reactivities are not related. The data obtained show the low selectivity of the S<sub>1</sub>′ subsite of subtilisin 72 and high specify of this subsite in α-chymotrypsin.</p>}}, author = {{Gololobov, Mikhail Yu and Voyushina, Tatyana L. and Stepanov, Valentin M. and Adlercreutz, Patrick}}, issn = {{0167-4838}}, keywords = {{Nucleophile specificity; Quantitative structure activity relationship; Substrate specificity; Subtilisin; α-chymotrypsin}}, language = {{eng}}, month = {{11}}, number = {{2}}, pages = {{188--192}}, publisher = {{Elsevier}}, series = {{BBA - Protein Structure and Molecular Enzymology}}, title = {{Nucleophile specificity in α-chymotrypsin- and subtilisin-(Bacillus subtilis strain 72) catalyzed reactions}}, url = {{http://dx.doi.org/10.1016/0167-4838(92)90006-Y}}, doi = {{10.1016/0167-4838(92)90006-Y}}, volume = {{1160}}, year = {{1992}}, }