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Tobias J. Erb (1979-)

Biologe

Name	Tobias J. Erb
Zeit	1979- (Lebensdaten)
Ort	Emmendingen (Geburtsort) Deutschland
Beruf	Biologe (charakteristischer Beruf)
Variante	Tobias Jürgen Erb
Weitere Angaben	Diss. Fakultät für Biologie an der Universität Freiburg im Breisgau
Datensatztyp	Person
GND-Nummer	138972133
Datensatz-ID	138972133
Beteiligt an alle anzeigen Adaptive laboratory evolution recruits the promiscuity of succinate semialdehyde dehydrogenase to repair different metabolic deficiencies Engineering new-to-nature biochemical conversions by combining fermentative metabolism with respiratory modules Revealing reaction intermediates in one-carbon elongation by thiamine diphosphate/CoA-dependent enzyme family Emergence of fractal geometries in the evolution of a metabolic enzyme Design and in vivo implementation of metabolic modules for synthetic carbon fixation Engineering a synthetic energy-efficient formaldehyde assimilation cycle in Escherichia coli Construction and modular implementation of the THETA cycle for synthetic CO2 fixation Structural insights into the iron nitrogenase complex Cell-free biosynthesis combined with deep learning accelerates de novo-development of antimicrobial peptides Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo From waste to health-supporting molecules : biosynthesis of natural products from lignin-, plastic- and seaweed-based monomers using metabolically engineered Streptomyces lividans A versatile active learning workflow for optimization of genetic and metabolic networks Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation Bioelektrokatalytische Cofaktor‐Regeneration und CO 2 ‐Fixierung in einem redoxaktiven Hydrogel durch stereoselektive C‐C‐Bindungsknüpfung Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation Eine modulare In‐vitro‐Plattform für die Produktion von Terpenen und Polyketiden aus CO 2 A Modular In Vitro Platform for the Production of Terpenes and Polyketides from CO 2 A Modular In Vitro Platform for the Production of Terpenes and Polyketides from CO 2 Benzylmalonyl-CoA dehydrogenase, an enzyme involved in bacterial auxin degradation A Modular In Vitro Platform for the Production of Terpenes and Polyketides from CO 2 A new-to-nature carboxylation module to improve natural and synthetic CO2 fixation Fünfter Gentechnologiebericht : Sachstand und Perspektiven für Forschung und Anwendung Awakening a latent carbon fixation cycle in Escherichia coli A common approach for absolute quantification of short chain CoA thioesters in prokaryotic and eukaryotic microbes Schöne neue Biologie? Synthetisch-biologische Ansätze zur CO2-Umwandlung Correction to: Using a marine microalga as a chassis for polyethylene terephthalate (PET) degradation Understanding Substrate Selectivity of Phoslactomycin Polyketide Synthase by Using Reconstituted in Vitro Systems Biochemical unity revisited: microbial central carbon metabolism holds new discoveries, multi-tasking pathways, and redundancies with a reason Oxalyl‐CoA Decarboxylase katalysiert die nukleophile ein‐Kohlenstoff‐Verlängerung von Aldehyden zu chiralen α‐Hydroxysäuren Titelbild: Oxalyl‐CoA Decarboxylase katalysiert die nukleophile ein‐Kohlenstoff‐Verlängerung von Aldehyden zu chiralen α‐Hydroxysäuren (Angew. Chem. 14/2020) Oxalyl‐CoA Decarboxylase Enables Nucleophilic One‐Carbon Extension of Aldehydes to Chiral α‐Hydroxy Acids Cover Picture: Oxalyl‐CoA Decarboxylase Enables Nucleophilic One‐Carbon Extension of Aldehydes to Chiral α‐Hydroxy Acids (Angew. Chem. Int. Ed. 14/2020) The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite Methanol assimilation in Methylobacterium extorquens AM1: demonstration of all enzymes and their regulation The ethylmalonyl-CoA pathway : a novel acetyl-CoA assimilation strategy

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Katalog der Deutschen Nationalbibliothek

Tobias J. Erb (1979-)

Adaptive laboratory evolution recruits the promiscuity of succinate semialdehyde dehydrogenase to repair different metabolic deficiencies

Engineering new-to-nature biochemical conversions by combining fermentative metabolism with respiratory modules

Revealing reaction intermediates in one-carbon elongation by thiamine diphosphate/CoA-dependent enzyme family

Emergence of fractal geometries in the evolution of a metabolic enzyme

Design and in vivo implementation of metabolic modules for synthetic carbon fixation

Engineering a synthetic energy-efficient formaldehyde assimilation cycle in Escherichia coli

Construction and modular implementation of the THETA cycle for synthetic CO2 fixation

Structural insights into the iron nitrogenase complex

Cell-free biosynthesis combined with deep learning accelerates de novo-development of antimicrobial peptides

Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo

From waste to health-supporting molecules : biosynthesis of natural products from lignin-, plastic- and seaweed-based monomers using metabolically engineered Streptomyces lividans

A versatile active learning workflow for optimization of genetic and metabolic networks

Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation

Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation

Bioelektrokatalytische Cofaktor‐Regeneration und CO 2 ‐Fixierung in einem redoxaktiven Hydrogel durch stereoselektive C‐C‐Bindungsknüpfung

Bioelectrocatalytic Cofactor Regeneration Coupled to CO 2 Fixation in a Redox‐Active Hydrogel for Stereoselective C−C Bond Formation

Eine modulare In‐vitro‐Plattform für die Produktion von Terpenen und Polyketiden aus CO 2

A Modular In Vitro Platform for the Production of Terpenes and Polyketides from CO 2

A Modular In Vitro Platform for the Production of Terpenes and Polyketides from CO 2

Benzylmalonyl-CoA dehydrogenase, an enzyme involved in bacterial auxin degradation

A Modular In Vitro Platform for the Production of Terpenes and Polyketides from CO 2

A new-to-nature carboxylation module to improve natural and synthetic CO2 fixation

Fünfter Gentechnologiebericht : Sachstand und Perspektiven für Forschung und Anwendung

Awakening a latent carbon fixation cycle in Escherichia coli

A common approach for absolute quantification of short chain CoA thioesters in prokaryotic and eukaryotic microbes

Schöne neue Biologie? Synthetisch-biologische Ansätze zur CO2-Umwandlung

Correction to: Using a marine microalga as a chassis for polyethylene terephthalate (PET) degradation

Understanding Substrate Selectivity of Phoslactomycin Polyketide Synthase by Using Reconstituted in Vitro Systems

Biochemical unity revisited: microbial central carbon metabolism holds new discoveries, multi-tasking pathways, and redundancies with a reason

Oxalyl‐CoA Decarboxylase katalysiert die nukleophile ein‐Kohlenstoff‐Verlängerung von Aldehyden zu chiralen α‐Hydroxysäuren

Titelbild: Oxalyl‐CoA Decarboxylase katalysiert die nukleophile ein‐Kohlenstoff‐Verlängerung von Aldehyden zu chiralen α‐Hydroxysäuren (Angew. Chem. 14/2020)

Oxalyl‐CoA Decarboxylase Enables Nucleophilic One‐Carbon Extension of Aldehydes to Chiral α‐Hydroxy Acids

Cover Picture: Oxalyl‐CoA Decarboxylase Enables Nucleophilic One‐Carbon Extension of Aldehydes to Chiral α‐Hydroxy Acids (Angew. Chem. Int. Ed. 14/2020)

The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite

Methanol assimilation in Methylobacterium extorquens AM1: demonstration of all enzymes and their regulation

The ethylmalonyl-CoA pathway : a novel acetyl-CoA assimilation strategy