Singh, Ashish Kumar ; Shivaji, Sisinthy (2010) A cold-active heat-labile t-RNA modification GTPase from a psychrophilic bacterium Pseudomonas syringae (Lz4W) Research in Microbiology, 161 (1). pp. 46-50. ISSN 0923-2508
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/j.resmic.2009.11.002
Abstract
A cold-active heat-labile t-RNA modification GTPase (TrmE) from psychrophilic bacterium Pseudomonas syringae (Lz4W) has been purified and characterized. The purified TrmE is a 53 kDa protein, has GTPase activity and hydrolyses only the oxy and deoxy forms of GTP but not the other nucleotide triphosphates. The enzyme exhibits optimal activity at 12-18 °C and retains 65% of its optimal activity at 4 °C, indicating that it is a cold-active enzyme. The enzyme is also heat-labile and loses 60% of its activity at 30 °C. This is the first report on the purification and characterization of a TrmE from a psychrophilic bacterium.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Pseudomonas syringae; Psychrophilic Bacterium; t-RNA Modification GTPase; TrmE; Cold-active Enzyme; Heat-labile Enzyme |
| ID Code: | 64307 |
| Deposited On: | 08 Oct 2011 04:11 |
| Last Modified: | 08 Oct 2011 04:11 |
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