Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies-Reference-Cited by-同舟云学术

Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies

Published:2016 Issue:7 Volume:7 Page:4492-4502
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Dick Markus¹²³⁴,Hartmann Rudolf⁵⁶⁷⁸⁴,Weiergräber Oliver H.⁵⁶⁷⁸⁴,Bisterfeld Carolin¹²³⁴,Classen Thomas⁹¹⁰⁷⁸⁴,Schwarten Melanie⁵⁶⁷⁸⁴,Neudecker Philipp⁵⁶⁷⁸⁴,Willbold Dieter⁵⁶⁷⁸⁴,Pietruszka Jörg¹²³⁴⁹

Affiliation:

1. Institute of Bioorganic Chemistry

2. Heinrich-Heine-Universität Düsseldorf im Forschungszentrum Jülich

3. 52426 Jülich

4. Germany

5. Institute of Complex Systems

6. ICS-6: Structural Biochemistry

7. Forschungszentrum Jülich GmbH

8. 52425 Jülich

9. Institute of Bio- and Geosciences

10. IBG-1: Biotechnology

Abstract

Understanding the deactivation mechanism of 2-deoxy-d-ribose-5-phosphate aldolase by its natural substrate leads to a single mutant showing complete acetaldehyde resistance.

Funder

Deutsche Forschungsgemeinschaft

Forschungszentrum Jülich

Heinrich-Heine-Universität Düsseldorf

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/SC/C5SC04574F

Reference59 articles.

1. Deoxyribose-5-phosphate aldolase as a synthetic catalyst