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Title: Substrate-Assisted Catalysis in the Reaction Catalyzed by Salicylic Acid Binding Protein 2 (SABP2), a Potential Mechanism of Substrate Discrimination for Some Promiscuous Enzymes

Abstract

Although one of an enzyme’s hallmarks is the high specificity for their natural substrates, substrate promiscuity has been reported more frequently. We know that promiscuous enzymes generally show different catalytic efficiencies to different substrates, but our understanding of the origin of such differences is still lacking. We report the results of quantum mechanical/molecular mechanical simulations and an experimental study of salicylic acid binding protein 2 (SABP2). SABP2 has promiscuous esterase activity toward a series of substrates but shows a high activity toward its natural substrate, methyl salicylate (MeSA). Finally, our results demonstrate that this enzyme may use substrate-assisted catalysis involving the hydroxyl group from MeSA to enhance the activity and achieve substrate discrimination.

Authors:
 [1];  [1];  [2];  [2];  [2];  [3];  [1]
  1. Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  2. Univ. of Tennessee, Knoxville, TN (United States)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1265709
Grant/Contract Number:  
AC05-00OR22725; ACI-1053575
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biochemistry
Additional Journal Information:
Journal Volume: 54; Journal Issue: 34; Journal ID: ISSN 0006-2960
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Yao, Jianzhuang, Guo, Haobo, Chaiprasongsuk, Minta, Zhao, Nan, Chen, Feng, Yang, Xiaohan, and Guo, Hong. Substrate-Assisted Catalysis in the Reaction Catalyzed by Salicylic Acid Binding Protein 2 (SABP2), a Potential Mechanism of Substrate Discrimination for Some Promiscuous Enzymes. United States: N. p., 2015. Web. doi:10.1021/acs.biochem.5b00638.
Yao, Jianzhuang, Guo, Haobo, Chaiprasongsuk, Minta, Zhao, Nan, Chen, Feng, Yang, Xiaohan, & Guo, Hong. Substrate-Assisted Catalysis in the Reaction Catalyzed by Salicylic Acid Binding Protein 2 (SABP2), a Potential Mechanism of Substrate Discrimination for Some Promiscuous Enzymes. United States. doi:10.1021/acs.biochem.5b00638.
Yao, Jianzhuang, Guo, Haobo, Chaiprasongsuk, Minta, Zhao, Nan, Chen, Feng, Yang, Xiaohan, and Guo, Hong. Wed . "Substrate-Assisted Catalysis in the Reaction Catalyzed by Salicylic Acid Binding Protein 2 (SABP2), a Potential Mechanism of Substrate Discrimination for Some Promiscuous Enzymes". United States. doi:10.1021/acs.biochem.5b00638. https://www.osti.gov/servlets/purl/1265709.
@article{osti_1265709,
title = {Substrate-Assisted Catalysis in the Reaction Catalyzed by Salicylic Acid Binding Protein 2 (SABP2), a Potential Mechanism of Substrate Discrimination for Some Promiscuous Enzymes},
author = {Yao, Jianzhuang and Guo, Haobo and Chaiprasongsuk, Minta and Zhao, Nan and Chen, Feng and Yang, Xiaohan and Guo, Hong},
abstractNote = {Although one of an enzyme’s hallmarks is the high specificity for their natural substrates, substrate promiscuity has been reported more frequently. We know that promiscuous enzymes generally show different catalytic efficiencies to different substrates, but our understanding of the origin of such differences is still lacking. We report the results of quantum mechanical/molecular mechanical simulations and an experimental study of salicylic acid binding protein 2 (SABP2). SABP2 has promiscuous esterase activity toward a series of substrates but shows a high activity toward its natural substrate, methyl salicylate (MeSA). Finally, our results demonstrate that this enzyme may use substrate-assisted catalysis involving the hydroxyl group from MeSA to enhance the activity and achieve substrate discrimination.},
doi = {10.1021/acs.biochem.5b00638},
journal = {Biochemistry},
number = 34,
volume = 54,
place = {United States},
year = {Wed Aug 05 00:00:00 EDT 2015},
month = {Wed Aug 05 00:00:00 EDT 2015}
}

Journal Article:
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Cited by: 7 works
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