Misc.

International journal
May, 2011

Cellular zwitterionic metabolite analogs simultaneously enhance reaction rate, thermostability, salt tolerance, and substrate specificity of alpha-glucosidase

BIOORGANIC & MEDICINAL CHEMISTRY
  • Eisuke Deguchi
  • ,
  • Kazuya Koumoto

Volume
19
Number
10
First page
3128
Last page
3134
Language
English
Publishing type
DOI
10.1016/j.bmc.2011.04.003
Publisher
PERGAMON-ELSEVIER SCIENCE LTD

We investigated the structural effects of metabolite analogs derived from a naturally-occurring zwitterionic metabolite, glycine betaine, on the activity of several hydrolases. The initial velocities of the hydrolases were enhanced by the addition of the solutes into the buffer solution. Based on a detailed study using alpha-glucosidases, the acceleration efficiency of the enzymatic activity was strongly induced by solutes possessing bulky and aliphatic ammonium cations, indicating that enhancement of activity by the solutes depended on their chemical structures. Kinetic analysis revealed that the acceleration of the hydrolysis reaction was related to both the decrement of K-m and increment of V-max values. Furthermore, the addition of the metabolite analogs enhanced not only the rate constant but also the thermostability, salt tolerance, and substrate specificity of alpha-glucosidase simultaneously through the reduction of conformational perturbation of the enzyme. (C) 2011 Elsevier Ltd. All rights reserved.

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Link information
DOI
https://doi.org/10.1016/j.bmc.2011.04.003
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/21524914
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000290299100009&DestApp=WOS_CPL
ID information
  • DOI : 10.1016/j.bmc.2011.04.003
  • ISSN : 0968-0896
  • eISSN : 1464-3391
  • Pubmed ID : 21524914
  • Web of Science ID : WOS:000290299100009

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