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Literature summary for 5.3.1.1 extracted from
- Cold adaptation of triosephosphate isomerase (2017), Biochemistry, 56, 4169-4176 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Moritella marina | P50921 | - |
- |
| Saccharomyces cerevisiae | P00942 | - |
- |
| Saccharomyces cerevisiae 288c | P00942 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TPI1 | - |
Saccharomyces cerevisiae |
| TpiA | - |
Moritella marina |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | comparison of Saccharomyces cerevisiae and Moritella marina enzymes to evaluate the temperature dependence of the activation free energy for differently adapted triosephosphate isomerases. Moritella marina TpiA displays a shift in enthalpy-entropy balance characteristic for cold-adapted proteins, due to a few surface-exposed protein loops that show differential mobilities in the two enzymes | Moritella marina |
| physiological function | comparison of Saccharomyces cerevisiae and Moritella marina enzymes to evaluate the temperature dependence of the activation free energy for differently adapted triosephosphate isomerases. Moritella marina TpiA displays a shift in enthalpy-entropy balance characteristic for cold-adapted proteins, due to a few surface-exposed protein loops that show differential mobilities in the two enzymes | Saccharomyces cerevisiae |
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