Literature DB >> 23702164

Evolutionary history and biotechnological future of carboxylases.

Lennart Schada von Borzyskowski1, Raoul G Rosenthal, Tobias J Erb.   

Abstract

Carbon dioxide (CO2) is a potent greenhouse gas whose presence in the atmosphere is a critical factor for global warming. At the same time atmospheric CO2 is also a cheap and readily available carbon source that can in principle be used to synthesize value-added products. However, as uncatalyzed chemical CO2-fixation reactions usually require quite harsh conditions to functionalize the CO2 molecule, not many processes have been developed that make use of CO2. In contrast to synthetical chemistry, Nature provides a multitude of different carboxylating enzymes whose carboxylating principle(s) might be exploited in biotechnology. This review focuses on the biochemical features of carboxylases, highlights possible evolutionary scenarios for the emergence of their reactivity, and discusses current, as well as potential future applications of carboxylases in organic synthesis, biotechnology and synthetic biology.
Copyright © 2013 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  CO(2)-Fixation; Enzyme evolution; Enzyme mechanisms; RubisCO; Synthetic biology

Mesh:

Substances:

Year:  2013        PMID: 23702164     DOI: 10.1016/j.jbiotec.2013.05.007

Source DB:  PubMed          Journal:  J Biotechnol        ISSN: 0168-1656            Impact factor:   3.307


  11 in total

Review 1.  Biochemical and synthetic biology approaches to improve photosynthetic CO2-fixation.

Authors:  Tobias J Erb; Jan Zarzycki
Journal:  Curr Opin Chem Biol       Date:  2016-07-09       Impact factor: 8.822

Review 2.  A short history of RubisCO: the rise and fall (?) of Nature's predominant CO2 fixing enzyme.

Authors:  Tobias J Erb; Jan Zarzycki
Journal:  Curr Opin Biotechnol       Date:  2017-08-29       Impact factor: 9.740

3.  Biosynthesis Based on One-Carbon Mixotrophy.

Authors:  Yaeseong Hong; An-Ping Zeng
Journal:  Adv Biochem Eng Biotechnol       Date:  2022       Impact factor: 2.635

4.  The LarB carboxylase/hydrolase forms a transient cysteinyl-pyridine intermediate during nickel-pincer nucleotide cofactor biosynthesis.

Authors:  Joel A Rankin; Shramana Chatterjee; Zia Tariq; Satyanarayana Lagishetty; Benoît Desguin; Jian Hu; Robert P Hausinger
Journal:  Proc Natl Acad Sci U S A       Date:  2021-09-28       Impact factor: 11.205

5.  A synthetic pathway for the fixation of carbon dioxide in vitro.

Authors:  Thomas Schwander; Lennart Schada von Borzyskowski; Simon Burgener; Niña Socorro Cortina; Tobias J Erb
Journal:  Science       Date:  2016-11-18       Impact factor: 47.728

6.  Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation.

Authors:  Florence Mus; Brian J Eilers; Alexander B Alleman; Burak V Kabasakal; Jennifer N Wells; James W Murray; Boguslaw P Nocek; Jennifer L DuBois; John W Peters
Journal:  Sci Rep       Date:  2017-08-03       Impact factor: 4.379

7.  Four amino acids define the CO2 binding pocket of enoyl-CoA carboxylases/reductases.

Authors:  Gabriele M M Stoffel; David Adrian Saez; Hasan DeMirci; Bastian Vögeli; Yashas Rao; Jan Zarzycki; Yasuo Yoshikuni; Soichi Wakatsuki; Esteban Vöhringer-Martinez; Tobias J Erb
Journal:  Proc Natl Acad Sci U S A       Date:  2019-06-26       Impact factor: 11.205

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

Authors:  Iria Bernhardsgrütter; Kristina Schell; Dominik M Peter; Farshad Borjian; David Adrian Saez; Esteban Vöhringer-Martinez; Tobias J Erb
Journal:  J Am Chem Soc       Date:  2019-06-14       Impact factor: 15.419

9.  Transcriptome of the coralline alga Calliarthron tuberculosum (Corallinales, Rhodophyta) reveals convergent evolution of a partial lignin biosynthesis pathway.

Authors:  Jan Y Xue; Katharine R Hind; Matthew A Lemay; Andrea Mcminigal; Emma Jourdain; Cheong Xin Chan; Patrick T Martone
Journal:  PLoS One       Date:  2022-07-14       Impact factor: 3.752

10.  Metal Ion Promiscuity and Structure of 2,3-Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae.

Authors:  Gerhard Hofer; Xiang Sheng; Simone Braeuer; Stefan E Payer; Katharina Plasch; Walter Goessler; Kurt Faber; Walter Keller; Fahmi Himo; Silvia M Glueck
Journal:  Chembiochem       Date:  2020-11-23       Impact factor: 3.164

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