Exploring substrate promiscuity of chlorophenol hydroxylase against biphenyl derivatives-Reference-Cited by-同舟云学术

Exploring substrate promiscuity of chlorophenol hydroxylase against biphenyl derivatives

Published:2015 Issue:105 Volume:5 Page:86817-86824
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Ren Hejun¹²³⁴⁵,Li Qingchao⁶⁷³⁴⁵,Fang Xuexun⁶⁷³⁴⁵,Yu Dahai⁶⁷³⁴⁵

Affiliation:

1. Key Laboratory of Ground Water Resources and Environment of the Ministry of Education

2. College of Environment and Resources

3. Jilin University

4. Changchun

5. P. R. China

6. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education

7. College of Life Science

Abstract

The substrate promiscuity of 2,4-dichlorophenol hydroxylase against biphenyl derivatives was explored. This enzyme may be used as a potentially useful catalyst in the bioremediation of aromatic contaminants.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/RA/C5RA16935F

Reference33 articles.

1. Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective

2. An example of enzymatic promiscuity: the Baylis–Hillman reaction catalyzed by a biotin esterase (BioH) from Escherichia coli

3. Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

4. Enzyme Promiscuity: Engine of Evolutionary Innovation

5. Recent Advances in Biocatalytic Promiscuity: Hydrolase-Catalyzed Reactions for Nonconventional Transformations

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