English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Awakening the Sleeping Carboxylase Function of Enzymes: Engineering the Natural CO2-Binding Potential of Reductases

MPS-Authors
/persons/resource/persons254137

Bernhardsgrütter,  Iria
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons263837

Schell,  Kristina
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254603

Peter,  Dominik
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons15496

Vohringer-Martinez,  Esteban
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons254247

Erb,  Tobias J.
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Bernhardsgrütter, I., Schell, K., Peter, D., Borjian, F., Adrian Saez, D., Vohringer-Martinez, E., et al. (2019). Awakening the Sleeping Carboxylase Function of Enzymes: Engineering the Natural CO2-Binding Potential of Reductases. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 141(25), 9778-9782. doi:10.1021/jacs.9b03431.


Cite as: https://hdl.handle.net/21.11116/0000-0008-BF22-B
Abstract
Developing new carbon dioxide (CO2) fixing enzymes is a prerequisite to
create new biocatalysts for diverse applications in chemistry,
biotechnology and synthetic biology. Here we used bioinformatics to
identify a "sleeping carboxylase function" in the superfamily of
medium-chain dehydrogenases/reductases (MDR), i.e. enzymes that possess
a low carboxylation side activity next to their original enzyme
reaction. We show that propionyl-CoA synthase from Erythrobacter sp.
NAP1, as well as an acrylyl-CoA reductase from Nitrosopumilus maritimus
possess carboxylation yields of 3 +/- 1 and 4.5 +/- 0.9%. We use
rational design to engineer these enzymes further into carboxylases by
increasing interactions of the proteins with CO2 and suppressing
diffusion of water to the active site. The engineered carboxylases show
improved CO2-binding and kinetic parameters comparable to naturally
existing CO2-fixing enzymes. Our results provide a strategy to develop
novel CO2-fixing enzymes and shed light on the emergence of natural
carboxylases during evolution.