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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
5.3.1.1
747198
A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase
Biochim. Biophys. Acta
1865
1423-1432
2017
Trichomonas vaginalis
28803140
5.3.1.1
747796
Characterization of triosephosphate isomerase from Mycoplasma gallisepticum
FEMS Microbiol. Lett.
362
fnv140
2015
Mycoplasma gallisepticum
26319024
5.3.1.1
747796
Characterization of triosephosphate isomerase from Mycoplasma gallisepticum
FEMS Microbiol. Lett.
362
fnv140
2015
Mycoplasma gallisepticum passage 15
26319024
5.3.1.1
747127
Cold adaptation of triosephosphate isomerase
Biochemistry
56
4169-4176
2017
Saccharomyces cerevisiae
28731682
5.3.1.1
747127
Cold adaptation of triosephosphate isomerase
Biochemistry
56
4169-4176
2017
Moritella marina
28731682
5.3.1.1
747127
Cold adaptation of triosephosphate isomerase
Biochemistry
56
4169-4176
2017
Saccharomyces cerevisiae 288c
28731682
5.3.1.1
747403
Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase
BMC Biochem.
16
20
2015
Saccharomyces cerevisiae
26334568
5.3.1.1
747543
Connecting active-site loop conformations and catalysis in triosephosphate isomerase Insights from a rare variation at residue 96 in the plasmodial enzyme
ChemBioChem
17
620-629
2016
Plasmodium falciparum
26762569
5.3.1.1
746661
Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity
Acta Crystallogr. Sect. F
72
490-499
2016
Trypanosoma brucei brucei
27303904
5.3.1.1
747871
Cytosolic triosephosphate isomerase from Arabidopsis thaliana is reversibly modified by glutathione on cysteines 127 and 218
Front. Plant Sci.
7
1942
2016
Arabidopsis thaliana
28066493
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