Study of the Enzymatic Activity of Arthrobacter ureafaciens Neuraminidase by Isothermal Titration Calorimetry

Study of the Enzymatic Activity of Arthrobacter ureafaciens Neuraminidase by Isothermal Titration... Isothermal titration calorimetry was used to determine the enzymatic activity and thermodynamic activation parameters of Arthrobacter ureafaciens sialidase with the sialyl substrates α‐2,3‐, α‐2,6‐sialyllactoses and α‐2,8‐sialic acid dimer. By monitoring the heat released during hydrolysis, the Michaelis constant (Km), catalytic rate constant (kcat), activation energy, activation Gibbs energy, enthalpy, and entropy for different monovalent sialyl conjugates were calculated and found to be consistent with those derived by chromatographic or colorimetric assays. The observed decreases in the activation energy and transition entropy of sialyllactoses were larger than the Michaelis activation parameters of lactose‐free di‐sialic acid because of the specific enzyme activity of A. ureafaciens sialidase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of the Chinese Chemical Society Wiley

Study of the Enzymatic Activity of Arthrobacter ureafaciens Neuraminidase by Isothermal Titration Calorimetry

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
© 2018 The Chemical Society Located in Taipei & Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim
ISSN
0009-4536
eISSN
2192-6549
D.O.I.
10.1002/jccs.201700303
Publisher site
See Article on Publisher Site

Abstract

Isothermal titration calorimetry was used to determine the enzymatic activity and thermodynamic activation parameters of Arthrobacter ureafaciens sialidase with the sialyl substrates α‐2,3‐, α‐2,6‐sialyllactoses and α‐2,8‐sialic acid dimer. By monitoring the heat released during hydrolysis, the Michaelis constant (Km), catalytic rate constant (kcat), activation energy, activation Gibbs energy, enthalpy, and entropy for different monovalent sialyl conjugates were calculated and found to be consistent with those derived by chromatographic or colorimetric assays. The observed decreases in the activation energy and transition entropy of sialyllactoses were larger than the Michaelis activation parameters of lactose‐free di‐sialic acid because of the specific enzyme activity of A. ureafaciens sialidase.

Journal

Journal of the Chinese Chemical SocietyWiley

Published: Jan 1, 2018

Keywords: ; ;

References

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