期刊
RESEARCH IN MICROBIOLOGY
卷 161, 期 1, 页码 46-50出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.resmic.2009.11.002
关键词
Pseudomonas syringae; Psychrophilic bacterium; t-RNA modification GTPase; TrmE; Cold-active enzyme; Heat-labile enzyme
类别
资金
- Council of Scientific and Industrial Research, New Delhi, Government of India
- CSIR
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 degrees C and retains 65% of its optimal activity at 4 degrees C, indicating that it is a cold-active enzyme. The enzyme is also heat-labile and loses 60% of its activity at 30 degrees C. This is the first report on the purification and characterization of a TrmE from a psychrophilic bacterium. (C) 2009 Elsevier Masson SAS. All rights reserved.
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