Temperature Effects on the Catalytic Efficiency, Rate Enhancement, and Transition State Affinity of Cytidine Deaminase, and the Thermodynamic Consequences for Catalysis of Removing a Substrate “Anchor”-Reference-Cited by-同舟云学术

Temperature Effects on the Catalytic Efficiency, Rate Enhancement, and Transition State Affinity of Cytidine Deaminase, and the Thermodynamic Consequences for Catalysis of Removing a Substrate “Anchor”

Published:2000-07-19 Issue:32 Volume:39 Page:9746-9753
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Snider Mark J.¹,Gaunitz Stefan¹,Ridgway Caroline¹,Short Steven A.¹,Wolfenden Richard¹

Affiliation:

1. Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, and Molecular Sciences, Venture 131, Glaxo-Wellcome, 5 Moore Drive, Research Triangle Park, North Carolina 27709

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi000914y

Reference40 articles.

1. The Temperature Dependence of Enzyme Rate Enhancements

2. Transition state stabilization by deaminases: Rates of nonenzymatic hydrolysis of adenosine and cytidine

3. Profound contribution of a carboxymethyl group to transition-state stabilization by cytidine deaminase: Mutation and rescue

4. Binding of pyrimidin-2-one ribonucleoside by cytidine deaminase as the transition-state analog 3,4-dihydrouridine and contribution of the 4-hydroxyl group to its binding affinity

5. Cytidine Deaminase. The 2·3 Å Crystal Structure of an Enzyme: Transition-state Analog Complex

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