A cold-active heat-labile t-RNA modification GTPase from a psychrophilic bacterium Pseudomonas syringae (Lz4W).
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.
Singh
Ashish Kumar
AK
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
Shivaji
Sisinthy
S
D003080:Cold Temperature; D004795:Enzyme Stability; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006358:Hot Temperature; D008970:Molecular Weight; D044224:Pseudomonas syringae / Q000201:enzymology*; D012343:RNA, Transfer / Q000378:metabolism*; D013379:Substrate Specificity; D013997:Time Factors
D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D020558:GTP Phosphohydrolases