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Literature summary for 2.2.1.1 extracted from

  • Jahromi, R.R.; Morris, P.; Martinez-Torres, R.J.; Dalby, P.A.
    Structural stability of E. coli transketolase to temperature and pH denaturation (2011), J. Biotechnol., 155, 209-216.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 10% non-cooperative loss of secondary structure as the temperature increases from 5°C to 50°C. This partial unfolding at moderately elevated temperatures may belinked to the enzyme activation observed at up to 55°C prior to the activity loss at higher temperatures. At 40-55°C the residual activity increases with incubation time and temperature when measured after re-cooling samples to 25°C, indicating that the protein undergoes an irreversible annealing, such that inactive forms of the enzyme are physically altered or activated by temperature Escherichia coli
58.3
-
 sharp transition in circular dichroism spectra, with appearance of aggregates Escherichia coli
60
-
 initial inactivation is slow with a first order rate constant of 0.007 per min, but after a lag phase a more rapid inactivation begins with a first order rate constant of 0.023 per min Escherichia coli
65
-
 inactivation follows single-exponential first-order kinetics with a rate constant of 0.181 per min Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
4.5 11 more than 50% of maximum activity Escherichia coli
6 8 more than 80% of maximum activity Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
3
-
 complete inactivation Escherichia coli
9
-
 high pH results in the formation of a native-like state that is only partially inactive. The apo-enzyme structure content also increases at pH 9 to converge on that of the holo-enzyme Escherichia coli