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Literature summary for 5.3.1.1 extracted from
- Introduction of a thermophile-sourced ion pair network in the fourth beta/alpha unit of a psychophile-derived triosephosphate isomerase from Methanococcoides burtonii significantly increases its kinetic thermal stability (2013), Biochim. Biophys. Acta, 1834, 1023-1033 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Methanococcoides burtonii |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 160000 | - |
gel filtration | Methanococcoides burtonii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanococcoides burtonii | Q12UK2 | - |
- |
| Methanococcoides burtonii DSM 6242 | Q12UK2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanococcoides burtonii |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 23000, SDS-PAGE | Methanococcoides burtonii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme lacks an intricate network of 4 ion pairs in its 4th beta/alpha unit, (beta/alpha)4. Iintroduction of a thermophile-sourced ion pair network in the fourth beta/alpha unit of a psychophile-derived triosephosphate isomerase from Methanococcoides burtonii significantly increases its kinetic thermal stability. The enzyme with the incorporated ion pair network, shows significantly higher apparent Tm values and also displays significantly higher kinetic thermal stability | Methanococcoides burtonii |
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Release 2023.1 (January 2023)
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