Literature summary for 5.3.1.1 extracted from

Guzman-Luna, V.; Quezada, A.G.; Diaz-Salazar, A.J.; Cabrera, N.; Perez-Montfort, R.; Costas, M.
The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes (2017), Proteins, 85, 571-579 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	analysis of chimera between Trypanosoma cruzi and Trypanosoma brucei brucei enzymes. The (betaalpha)2 motif of Trypanosoma cruzi TIM inserted into Trypanosoma brucei brucei TIM increases the kinetic stability. The presence of the (betaalpha)2 motif of Trypanosoma brucei brucei TIM inserted into Trypanosoma cruzi TIM gives a chimerical protein difficult to purify in soluble form and with a significantly reduced kinetic stability	Trypanosoma brucei brucei
additional information	analysis of chimera between Trypanosoma cruzi and Trypanosoma brucei brucei enzymes. The (betaalpha)2 motif of Trypanosoma cruzi TIM inserted into Trypanosoma brucei brucei TIM increases the kinetic stability. The presence of the (betaalpha)2 motif of Trypanosoma brucei brucei TIM inserted into Trypanosoma cruzi TIM gives a chimerical protein difficult to purify in soluble form and with a significantly reduces kinetic stability	Trypanosoma cruzi
S43P	mutation increases the free energy of the transition state by 17.7 kJ/mol	Trypanosoma brucei brucei

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei brucei	P04789	-	-
Trypanosoma cruzi	P52270	-	-

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Release 2023.1 (January 2023)