Literature summary for 5.3.1.1 extracted from

Krause, M.; Kiema, T.R.; Neubauer, P.; Wierenga, R.K.
Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity (2016), Acta Crystallogr. Sect. F, 72, 490-499 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Trypanosoma brucei brucei

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of wild-type and mutants Q65L and E23G/A70T/S96F/A178V. Mutation Q65L contributes to small structural rearrangements near Asn11 of loop 1, which correlate with different ligand-binding properties. Its Leu65 side chain is involved in van der Waals interactions with neighbouring hydrophobic side-chain moieties	Trypanosoma brucei brucei

Protein Variants

Protein Variants	Comment	Organism
E23G/A70T/S96F/A178V	mutant facilitates better growth of a Escherichia coli L-arabinose isomerase knockout strain in medium supplemented with 40 mM L-arabinose. Mutant shows increased thermostability	Trypanosoma brucei brucei
Q65L	mutant facilitates better growth of a Escherichia coli L-arabinose isomerase knockout strain in medium supplemented with 40 mM L-arabinose. Mutant shows increased thermostability	Trypanosoma brucei brucei

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei brucei	P04789	-	-

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Release 2023.1 (January 2023)