Biocatalytic Oxidative CC Bond Formation Catalysed by the Berberine Bridge Enzyme: Optimal Reaction Conditions (Q57978260)

From Wikidata

Jump to navigation Jump to search

scholarly article by Verena Resch et al published 26 August 2011 in Advanced Synthesis & Catalysis

Language	Label	Description	Also known as
English	Biocatalytic Oxidative CC Bond Formation Catalysed by the Berberine Bridge Enzyme: Optimal Reaction Conditions	scholarly article by Verena Resch et al published 26 August 2011 in Advanced Synthesis & Catalysis

Statements

scholarly article

0 references

Biocatalytic Oxidative CC Bond Formation Catalysed by the Berberine Bridge Enzyme: Optimal Reaction Conditions (English)

0 references

0 references

Wolfgang Kroutil

object named as

Wolfgang Kroutil

5

0 references

Peter Macheroux

object named as

Peter Macheroux

4

0 references

author name string

Verena Resch

1

0 references

Joerg H. Schrittwieser

2

0 references

Silvia Wallner

3

0 references

publication date

26 August 2011

0 references

Advanced Synthesis & Catalysis

0 references

353

0 references

13

0 references

2377-2383

0 references

Synthesizing our future

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

New opportunities for biocatalysis: making pharmaceutical processes greener.

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Dispelling the myths--biocatalysis in industrial synthesis

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Recent progress in stereoselective synthesis with aldolases

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Chemoenzymatic synthesis of differentially protected 3-deoxysugars

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

The enzymatic asymmetric conjugate umpolung reaction

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Thiamin diphosphate in biological chemistry: exploitation of diverse thiamin diphosphate-dependent enzymes for asymmetric chemoenzymatic synthesis.

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Enantioselective intermolecular aldehyde-ketone cross-coupling through an enzymatic carboligation reaction.

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Laccases: blue enzymes for green chemistry.

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

A concerted mechanism for berberine bridge enzyme

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzyme

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Laboratory evolution of cytochrome p450 BM-3 monooxygenase for organic cosolvents

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Biocatalysis in semi-aqueous and nearly anhydrous conditions.

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Understanding enzyme immobilisation

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Immobilised enzymes: science or art?

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

6-S-Cysteinylation of Bi-covalently Attached FAD in Berberine Bridge Enzyme Tunes the Redox Potential for Optimal Activity

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Heterologous expression of alkaloid biosynthetic genes--a review

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method

1 reference

https://api.crossref.org/works/10.1002%2FADSC.201100233

21 January 2018

Identifiers

10.1002/ADSC.201100233

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q57978260&oldid=2030867175"