Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential-Reference-Cited by-同舟云学术

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Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential

Published:2015 Issue:62 Volume:5 Page:49987-49995
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Abood Amira¹²³⁴⁵,Al-Fahad Ahmed¹²³⁴⁶,Scott Alan¹²³⁴,Hosny Alaa El-Dein M. S.⁷⁸⁹¹⁰¹¹,Hashem Amal M.⁵¹²¹⁰¹¹,Fattah Azza M. A.⁵¹²¹⁰¹¹,Race Paul R.¹³³⁴,Simpson Thomas J.¹²³⁴,Cox Russell J.¹²³⁴¹⁴

Affiliation:

1. School

2. of Chemistry

3. University of Bristol

4. UK

5. Chemistry of Natural and Microbial Products Department

6. Chemistry Department

7. Microbiology Department

8. Faculty of Pharmacy

9. Cairo University

10. Cairo

11. Egypt

12. National Research Centre

13. School of Biochemistry

14. Institut für Organische Chemie

Abstract

Achieving regio-specific hydroxylation of aromatic compounds remains a major challenge in synthetic chemistry.

Funder

Biotechnology and Biological Sciences Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/RA/C5RA06693J

Reference26 articles.

1. Enzymatic hydroxylation of aromatic compounds

2. Flavin dependent monooxygenases

3. Synthesis of 3-tert-butylcatechol by an engineered monooxygenase

4. Genetic, molecular, and biochemical basis of fungal tropolone biosynthesis

5. Synthesis of the Azaphilones Using Copper-Mediated Enantioselective Oxidative Dearomatization

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