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Nucleophile specifi...
Nucleophile specificity in α-chymotrypsin- and subtilisin-(Bacillus subtilis strain 72) catalyzed reactions
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- Gololobov, Mikhail Yu (author)
- Lund University
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- Voyushina, Tatyana L. (author)
- State Research Institute of Genetics and Selection of Industrial Microorganisms of NRC «Kurchatov Institute»
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- Stepanov, Valentin M. (author)
- State Research Institute of Genetics and Selection of Industrial Microorganisms of NRC «Kurchatov Institute»
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- Adlercreutz, Patrick (author)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 1992
- 1992
- English 5 s.
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In: BBA - Protein Structure and Molecular Enzymology. - 0167-4838. ; 1160:2, s. 188-192
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http://dx.doi.org/10...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
Keyword
- Nucleophile specificity
- Quantitative structure activity relationship
- Substrate specificity
- Subtilisin
- α-chymotrypsin
Publication and Content Type
- art (subject category)
- ref (subject category)
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