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References (14)
-
J. Knapp, A. Callely, J. Mainprize (1982)
The microbial degradation of morpholineJournal of Applied Microbiology, 52
-
(2008)
The effect of two alkane hydroxylase genes on crude oil degradation by Acinetobacte calcoaceticus isolated from oil contaminated sits in Persian Gulf -
Hasan Mehdi, E. Giti (2008)
Investigation of alkane biodegradation using the microtiter plate method and correlation between biofilm formation, biosurfactant production and crude oil biodegradationInternational Biodeterioration & Biodegradation, 62
-
S. Vuilleumier, M. Pagni (2002)
The elusive roles of bacterial glutathione S-transferases: new lessons from genomesApplied Microbiology and Biotechnology, 58
-
J. Knapp, G. Emtiazl, S. Yusoff, S. Heron (1996)
The utilization of morpholine as a sole nitrogen source by Gram‐negative bacteriaLetters in Applied Microbiology, 23
-
R. Zablotowicz, R. Hoagland, M. Locke, W. Hickey (1995)
Glutathione-s-transferase activity and metabolism of glutathione conjugates by rhizosphere bacteriaApplied and Environmental Microbiology, 61
-
W. Stevens, K. Skov (1965)
A rapid spectrophotometric method for determining parts per million of morpholine in boiler waterAnalyst, 90
-
W. Habig, W. Jakoby (1981)
Assays for differentiation of glutathione S-transferases.Methods in enzymology, 77
-
P. Santos, G. Mignogna, H. Heipieper, E. Zennaro (2002)
Occurrence and properties of glutathione S-transferases in phenol-degrading Pseudomonas strains.Research in microbiology, 153 2
-
E. Tocheva, Pascal Fortin, L. Eltis, M. Murphy (2006)
Structures of Ternary Complexes of BphK, a Bacterial Glutathione S-Transferase That Reductively Dechlorinates Polychlorinated Biphenyl Metabolites*Journal of Biological Chemistry, 281
-
Jeremy Knapp, Alison Whytell (1990)
The biodegradation of morpholine in river water and activated sludge.Environmental pollution, 68 1-2
-
F. Bartels, S. Backhaus, E. Moore, K. Timmis, B. Hofer (1999)
Occurrence and expression of glutathione-S-transferase-encoding bphK genes in Burkholderia sp. strain LB400 and other biphenyl-utilizing bacteria.Microbiology, 145 ( Pt 10)
-
Pascal Fortin, Geoff Horsman, Hao Yang, L. Eltis (2006)
A Glutathione S-Transferase Catalyzes the Dehalogenation of Inhibitory Metabolites of Polychlorinated BiphenylsJournal of Bacteriology, 188
-
S. Vuilleumier (1997)
Bacterial glutathione S-transferases: what are they good for?Journal of Bacteriology, 179
- Publisher
- Wiley
- Copyright
- Copyright © 2009 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1860-6768
- eISSN
- 1860-7314
- DOI
- 10.1002/biot.200800238
- pmid
- 19194977
- Publisher site
- See Article on Publisher Site
Abstract
Glutathione S‐transferases (GSTs) constitute a large family of enzymes that catalyze the addition of glutathione to endogenous, or xenobiotic, often toxic electrophilic compounds. The effect of this enzyme in facilitating polychlorinated biphenyls degradation has been studied previously. Here the effects of induced cell‐free extracts of Acinetobacter calcoaceticus and Pseudomonas aeruginosa (grown on hexadecane), and E. coli BL21 (induced with pGEX‐2T plasmid on isothiopropylgalactoside) were recruited to facilitate morpholine degradation by Mycobacterium and were compared with non‐induced strains. The results showed that all induced strains had significantly more GST activity compared to non‐induced ones, and the strain with most GST activity, A. calcoaceticus BS, removed morpholine faster. Eukaryotic GST gene expressed in E. coli BL21 also could facilitate morpholine degradation by Mycobacterium, The same experiments performed with cell‐free extracts of non‐induced cells did not show any significant effects on morpholine removal. These results showed that there is a correlation between GST activity and acceleration of morpholine degradation.
Journal
Biotechnology Journal – Wiley
Published: Feb 1, 2009
Keywords: ; ; ;