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Nucleophile specificity in α-chymotrypsin- and subtilisin-(Bacillus subtilis strain 72) catalyzed reactions

Gololobov, Mikhail Yu; Voyushina, Tatyana L.; Stepanov, Valentin M. and Adlercreutz, Patrick LU (1992) In Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 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.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Nucleophile specificity, Quantitative structure activity relationship, Substrate specificity, Subtilisin, α-chymotrypsin
in
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
volume
1160
issue
2
pages
5 pages
publisher
Elsevier
external identifiers
  • 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
2019-08-23 02:22:39
@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> &lt; GlyNH<sub>2</sub> &lt; l-AlaNH<sub>2</sub> &lt; l-ScrNH<sub>2</sub> &lt; l-ThrNH<sub>2</sub> &lt; l-HisNH<sub>2</sub> &lt; l-ValNH<sub>2</sub> &lt; l-LcuNH<sub>2</sub> &lt; l-TrpNH<sub>2</sub> &lt; l-MetNH<sub>2</sub> &lt; l-NvaNH<sub>2</sub> &lt; l-PheNH<sub>2</sub> &lt; l-IleNH<sub>2</sub> &lt; l-TyrNH<sub>2</sub> &lt; l-ArgNH<sub>2</sub>. In reactions catalyzed by subtilisin 72, the reactivities increase as follows: l-LeuNH<sub>2</sub> &lt; l- IleNH<sub>2</sub> &lt; l-ThrNH<sub>2</sub> &lt; l-ArgNH<sub>2</sub> &lt; l-TrpNH<sub>2</sub> &lt; l-NvaNH<sub>2</sub> &lt; l-ValNH<sub>2</sub> &lt; l-MctNH<sub>2</sub> &lt; l-AlaNH<sub>2</sub> &lt; l-ScrNH<sub>2</sub> &lt; d-AlaNH<sub>2</sub> &lt; 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},
  keyword      = {Nucleophile specificity,Quantitative structure activity relationship,Substrate specificity,Subtilisin,α-chymotrypsin},
  language     = {eng},
  month        = {11},
  number       = {2},
  pages        = {188--192},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular},
  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},
  volume       = {1160},
  year         = {1992},
}