PMID- 26672451
OWN - NLM
STAT- MEDLINE
DCOM- 20161011
LR  - 20170807
IS  - 1879-0909 (Electronic)
IS  - 0141-0229 (Linking)
VI  - 82
DP  - 2016 Jan
TI  - 2,4-Dichlorophenol hydroxylase for chlorophenol removal: Substrate specificity 
      and catalytic activity.
PG  - 74-81
LID - S0141-0229(15)30043-0 [pii]
LID - 10.1016/j.enzmictec.2015.08.008 [doi]
AB  - Chlorophenols (CPs) are common environmental pollutants. As such, different 
      treatments have been assessed to facilitate their removal. In this study, 
      2,4-dichlorophenol (2,4-DCP) hydroxylase was used to systematically investigate 
      the activity and removal ability of 19CP congeners at 25 and 0  degrees C. Results 
      demonstrated that 2,4-DCP hydroxylase exhibited a broad substrate specificity to 
      CPs. The activities of 2,4-DCP hydroxylase against specific CP congeners, 
      including 3-CP, 2,3,6-trichlorophenol, 2-CP, and 2,3-DCP, were higher than those 
      against 2,4-DCP, which is the preferred substrate of previously reported 2,4-DCP 
      hydroxylase. To verify whether cofactors are necessary to promote hydroxylase 
      activity against CP congeners, we added FAD and found that the added FAD induced 
      a 1.33-fold to 5.13-fold significant increase in hydroxylase activity against 
      different CP congeners. The metabolic pathways of the CP degradation in the 
      enzymatic hydroxylation step were preliminarily proposed on the basis of the 
      analyses of the enzymatic activities against 19CP congeners. We found that the 
      high activity and removal rate of 2,4-DCP hydroxylase against CPs at 0  degrees C enhance 
      the low-temperature-adaptability of this enzyme to the CP congeners; as such, the 
      proposed removal process may be applied to biochemical, bioremediation, and 
      industrial processes, particularly in cold environments.
CI  - Copyright (c) 2015 Elsevier Inc. All rights reserved.
FAU - Ren, Hejun
AU  - Ren H
AD  - Key Laboratory of Ground Water Resources and Environment of the Ministry of 
      Education, College of Environment and Resources, Jilin University, 2519 Jiefang 
      Road, Changchun 130021, PR China.
FAU - Li, Qingchao
AU  - Li Q
AD  - Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, 
      College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, 
      PR China.
FAU - Zhan, Yang
AU  - Zhan Y
AD  - Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, 
      College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, 
      PR China.
FAU - Fang, Xuexun
AU  - Fang X
AD  - Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, 
      College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, 
      PR China.
FAU - Yu, Dahai
AU  - Yu D
AD  - Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, 
      College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, 
      PR China. Electronic address: yudahai@jlu.edu.cn.
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20150820
PL  - United States
TA  - Enzyme Microb Technol
JT  - Enzyme and microbial technology
JID - 8003761
RN  - 0 (Bacterial Proteins)
RN  - 0 (Chlorophenols)
RN  - 0 (Coenzymes)
RN  - 0 (Environmental Pollutants)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 146-14-5 (Flavin-Adenine Dinucleotide)
RN  - EC 1.- (Mixed Function Oxygenases)
RN  - EC 1.14.13.- (2,4-dichlorophenol hydroxylase)
SB  - IM
MH  - Bacterial Proteins/*metabolism
MH  - Biodegradation, Environmental
MH  - Catalysis
MH  - Chlorophenols/*metabolism
MH  - Chromatography, High Pressure Liquid
MH  - Coenzymes/metabolism
MH  - Cold Temperature
MH  - Environmental Pollutants/metabolism
MH  - Escherichia coli
MH  - Flavin-Adenine Dinucleotide/metabolism
MH  - Mixed Function Oxygenases/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Substrate Specificity
OTO - NOTNLM
OT  - 2,4-Dichlorophenol hydroxylase
OT  - Chlorophenols
OT  - Cold-active
OT  - Removal
OT  - Substrate specificity
EDAT- 2015/12/18 06:00
MHDA- 2016/10/12 06:00
CRDT- 2015/12/18 06:00
PHST- 2015/06/26 00:00 [received]
PHST- 2015/08/11 00:00 [revised]
PHST- 2015/08/11 00:00 [accepted]
PHST- 2015/12/18 06:00 [entrez]
PHST- 2015/12/18 06:00 [pubmed]
PHST- 2016/10/12 06:00 [medline]
AID - S0141-0229(15)30043-0 [pii]
AID - 10.1016/j.enzmictec.2015.08.008 [doi]
PST - ppublish
SO  - Enzyme Microb Technol. 2016 Jan;82:74-81. doi: 10.1016/j.enzmictec.2015.08.008. 
      Epub 2015 Aug 20.