[A comparative study of the thermal stability of phenylalanyl tRNA synthetase from Escherichia coli MRE-600 and Thermus thermophilus HB 8].
The thermal stability of phenylalanyl-tRNA-synthetase (PTS) from E. coli and T.thermophilus HB 8 was studied in solution at various conditions by scanning microcalorimetry. It has been shown that the value of heating rate, concentration of the enzyme and Mg2+ ions in the solution affects the parameters of thermal denaturation of both enzymes. The higher thermal stability of PTS from T. thermophilus was observed as well as the independence of its properties upon broad variations of experimental conditions. The role of thermostability of the enzymes are discussed with respect to the biological properties of E. coli and T.thermophilus.
Frank
E G
EG
Reshetnikova
L S
LS
Ankilova
V N
VN
Chernaia
M M
MM
Esipova
N G
NG
D002152:Calorimetry, Differential Scanning; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D007700:Kinetics; D008274:Magnesium; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism; D016963:Thermus thermophilus / Q000201:enzymology*
D010652:Phenylalanine-tRNA Ligase; D008274:Magnesium
Sravnitel'noe issledovanie termostabil'nosti fenilalanil-tRNK-sintetaz iz Escherichia coli MRE-600 i Thermus thermophilus HB 8.