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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00942
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5.3.1.1 triose-phosphate isomeraseSpecify your search results
Word Map
- 5.3.1.1
- giardia
-
assemblage
- aldolase
- duodenalis
- dihydroxyacetone
- enolase
- phosphoglycerate
-
zoonotic
-
barrel
-
fecal
- trypanosoma
-
multilocus
- fructose
- giardiasis
- dhap
- cryptosporidium
- brucei
-
protozoan
- isomerases
- gapdh
-
province
- cysts
- malate
-
stool
- lamblia
- methylglyoxal
-
phosphofructokinase
- cruzi
- schistosoma
-
enediolate
- 2-phosphoglycolate
- parvum
-
hemolytic
- intestinalis
- fructose-1,6-bisphosphate
-
deamidation
- alpha-enolase
- 1,6-bisphosphate
-
glucosephosphate
-
tim-barrel
-
hungarian
- hominis
- phosphite
-
dianion
-
phosphoglucose
- glycosomes
-
enzymopathy
-
fructose-bisphosphate
-
ige-binding
-
subgenotype
- diagnostics
- synthesis
- analysis
- biofuel production
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
triosephosphate isomerase, triose phosphate isomerase, triose-phosphate isomerase, tctim, pftim, gltim, monotim, pfutim, cp 25, cytoplasmic tpi, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CP 25
-
-
-
-
D-glyceraldehyde-3-phosphate ketol-isomerase
-
-
-
-
Isomerase, triose phosphate
-
-
-
-
Lactacin B inducer protein
-
-
-
-
monoTIM
-
-
-
-
PfTIM
-
-
-
-
Phosphotriose isomerase
-
-
-
-
TIM
Triose phosphate isomerase
-
-
-
-
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
TIM
-
-
-
-
Triosephosphate isomerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Glyceraldehyde 3-phosphate = glycerone phosphate
in situ magnetic resonance probes of the enzyme-bound substrates to test the question of whether the equilibrium concentrations are perturbed by the enzyme. In the exergonic conversion of glycerinaldehyde 3-phosphate to dihydroxyacetone phosphate the high discrimination against solvent isotope uptake is consistent with chemistry protected by a water-tight active-site loop, therefore introducing asymmetry into the reversible reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
CAS REGISTRY NUMBER
COMMENTARY
9023-78-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
dihydroxyacetone 3-phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
substrate binding perturbs residues Asn10, His95, Ser100, Glu129-Glu133, Val167-Ala186, Asn213, and Leu230-Leu126 that either are near the ligand or have direct contact with the ligand
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
additional information
?
-
the effect of bound phosphite dianion on the activation barrier is small, in comparison to the much larger intrinsic phosphodianion and phosphite dianion binding energy utilized to stabilize the transition states for TIM-catalyzed deprotonation of glyceraldehyde-3-phosphate and glyceraldehyde-phosphite dianion complex, respectively
-
-
?
additional information
?
-
the substrate is locked in a protein cage with the phosphodianion occluded from interaction with solvent water, and ion-paired to the surface alkyl ammonium side chain of residue K12. The neutral imidazole side chain of H95 interacts with the carbonyl oxygen of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Phosphoglycolate
-
strong, competitive. Inhibition results in a large decrease in the unfolding rate constant of the protein. 2-phosphoglycolate shows similar binding affinities in the transition states for the rate-limiting steps of the forward and backward reactions, implicating that both transition states resemble each other in the active site architecture
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
D-glyceraldehyde 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
1.09
D-glyceraldehyde 3-phosphate
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C
1.2
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C
1.26
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C
2.44
D-glyceraldehyde 3-phosphate
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C
4
dihydroxyacetone 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
0.3
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126S
0.8
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126A
1.1
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
50
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.69
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C
1.04
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C
520
D-glyceraldehyde 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
4160
D-glyceraldehyde 3-phosphate
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C
7020
D-glyceraldehyde 3-phosphate
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C
135
dihydroxyacetone 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
0.6
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
1100
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126S
3100
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126A
7300
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
730
D-glyceraldehyde 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
34
dihydroxyacetone 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
0.012
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
6600
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
2-Phosphoglycolate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
1.1
2-Phosphoglycolate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
additional information
dimer
-
the low stability of the monomers is neither the only, nor the main, cause for the dimeric nature of the enzyme
additional information
determination of conformational dynamics of the enzyme, in solid state and in solution, with or without bound ligand, by NMR analysis, detailed overview
additional information
-
determination of conformational dynamics of the enzyme, in solid state and in solution, with or without bound ligand, by NMR analysis, detailed overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, 200 mg/ml protein with ligand in a ratio of 5:1 in 50 mM Tris-HCl, 50 mM NaCl, and 1 mM EDTA, pH 6.8, 4°C, is mixed with 40% w/v PEG 4000 as precipitant, X-ray diffraction structure determination and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I170A
effect of the mutation on the relative electrostatic contribution of the residue is negligible. Mutation results in increases in the activation barriers for deprotonation of substrate
I170A/L230A
effect of the mutation on the relative electrostatic contribution of the residue is negligible. Mutation results in increases in the activation barriers for deprotonation of substrate
K17A/Y46A/D48F/Q82A/D85S
mutation of residues in the dimer interface of enzyme
K17L/Y46F/D48F/Q82F/D85L
mutation of residues in the dimer interface of enzyme. Decrease in catalytic efficiency by 4 orders of magnitude
K17L/Y46F/D48Y/Q82A/D85A
mutation of residues in the dimer interface of enzyme. Decrease in catalytic efficiency by 4 orders of magnitude
K17P/Y46A/D48L/Q82T/D85A
mutation of residues in the dimer interface of enzyme
L230A
effect of the mutation on the relative electrostatic contribution of the residue is negligible. Mutation results in increases in the activation barriers for deprotonation of substrate
S211A
mutation eliminates intraloop hydrogen bonds to the side-chain hydroxyl, 60fold decrease in kcat/Km
S211G
mutation eliminates intraloop hydrogen bonds to the side-chain hydroxyl, leading to small changes in the kinetic parameters
Y208A
main effect of mutations is to cause a reduction in the total intrinsic dianion binding energy
Y208F
mutation eliminates the intraloop hydrogen bond between the hydroxyl group of Y208 and the amide nitrogen of A176. Enzyme activity is reduced by ca. 50fold compared to the Y208A and Y208S mutants
Y208S
main effect of mutations is to cause a reduction in the total intrinsic dianion binding energy
Y208T
main effect of mutations is to cause a reduction in the total intrinsic dianion binding energy
C126A
-
turnover number for D-glyceraldehyde 3-phosphate is 1.5fold lower than the wild-type value, KM-value for D-glyceraldehyde 3-phosphate is 1.4fold lower than the wild-type value, turnover number for dihydroxyacetone phosphate is 4.3fold lower than the wild-type value, KM-value for dihydroxyacetone phosphate is 3.7fold lower than the wild-type value
C126S
-
mutant enzyme shows greater susceptibility to thermal denaturation than wild-type enzyme, turnover number for dihydroxyacetone phosphate is 8.3fold lower than the wild-type value, KM-value for dihydroxyacetone phosphate is 3.5fold lower than the wild-type value
D225Q
-
mutation causes minor drops in Km and kcat value without changes catalytic efficiency. Temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain
K12G
-
the mutation results in a ca. 50fold increase in Km for the substrate glyceraldehyde 3-phosphate (GAP) and a 60fold increase in Ki for competitive inhibition by 2-phosphoglycolate, a 12000fold decrease in kcat for isomerization of GAP, and a 6000000fold decrease in kcat/Km for GAP
additional information
additional information
mutation of five residues in the dimer interface of enzyme. Obtained proteins are soluble, dimeric, and compact. Proteins obtained from direct evolution experiments show wild-type-like catalytic activity, while their stability is decreased. In silico-designed proteins are very stable dimers that bind substrate with a wild-type-like Km value, albeit they exhibit a very low kcat
additional information
-
mutation of five residues in the dimer interface of enzyme. Obtained proteins are soluble, dimeric, and compact. Proteins obtained from direct evolution experiments show wild-type-like catalytic activity, while their stability is decreased. In silico-designed proteins are very stable dimers that bind substrate with a wild-type-like Km value, albeit they exhibit a very low kcat
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63
if denaturation is carried out at temperatures above 64.0°C, a partially folded species is formed in a time short enough to avoid the occurence of deleterious aggregation reactions
additional information
additional information
denaturation of the enzyme likely consists of an initial first-order reaction that forms thermally unfolded enzyme, followed by irreversibility-inducing reactions which are probably linked to aggregation of the unfolded protein
additional information
-
denaturation of the enzyme likely consists of an initial first-order reaction that forms thermally unfolded enzyme, followed by irreversibility-inducing reactions which are probably linked to aggregation of the unfolded protein
additional information
-
slow temperature-induced unfolding of yeast TIM shows three kinetic phases. A complex mechanism involving off-pathway intermediates or parallel pathways may be operating. beta-Strand-type residual structure appears below pH 8.0, and is likely to be associated with increased irreversible aggregation of the unfolded protein, which accelerates the refolding process
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
6 M, incubation times longer thah 10 min lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme
urea
-
8 M, incubation times longer than 5 h lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type enzyme and mutant enzymes C126S and C126A in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the refolding reaction of the thermally denatured enzyme obeys second-order kinetics and leads to the formation of dimer nativelike enzyme, dimerization is coupled to the regain of a large amount of secondary structure
inhibitor 2-phosphoglycolate brings about a large decrease in the unfolding rate constant of the protein. Thermodynamics of binding reveal a dimeric transition state
-
reversible denaturation and renaturation of the homodimeric enzyme induced by urea and guanidine-HClm renaturation is fully reversible. Unfolding experiments do not reach an equilibrium, owing to a very slow dissociation and/or unfolding process. By contrast, equilibrium is reached in the refolding direction
-
study on the effect of viscosity in the unfolding and refolding of enzyme. Two transitions indicate a three-state model with a monomeric intermediate. The bimolecular association producing the native dimer is limited by diffusional events of the polypeptide chains through the solvent
-
study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Entamoeba histolytica. Monomer unfolding is reversible for both enzymes, the dissociation step is reversible in yeast and irreversible in Entamoeba histolytica. Monomer unfolding induced by high pressure in presence of guanidinium hydrochloride is reversible. In the absence of denaturants, pressure would induce monomer unfolding prior to dimer dissociation
-
temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain
-
thermally unfolded protein refolds faster at pH 6.7 than at pH 8.0 and TIM refolds faster from the denatured state with residual structure
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krietsch, W.K.G.
Triosephosphate isomerase from yeast
Methods Enzymol.
41B
434-438
1975
Saccharomyces cerevisiae
-
Nickbarg, E.B.; Knowles, J.R.
Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli
Biochemistry
27
5939-5947
1988
Saccharomyces cerevisiae
Carza-Ramos, G.; Perez-Montfort, R.; Rojo-Dominguez, A.; de Gomez-Puyou, M.T.; Gomez-Puyou, A.
Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase
Eur. J. Biochem.
241
114-120
1996
Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Schizosaccharomyces pombe
Najera, H.; Costas, M.; Fernandez-Velasco, D.A.
Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme
Biochem. J.
370
785-792
2003
Saccharomyces cerevisiae
Benitez-Cardoza, C.G.; Rojo-Dominguez, A.; Hernandez-Arana, A.
Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein
Biochemistry
40
9049-9058
2001
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae
Gonzalez-Mondragon, E.; Zubillaga, R.A.; Saavedra, E.; Chanez-Cardenas, M.E.; Perez-Montfort, R.; Hernandez-Arana, A.
Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability
Biochemistry
43
3255-3263
2004
Saccharomyces cerevisiae
Vazquez-Perez, A.R.; Fernandez-Velasco, D.A.
Pressure and denaturants in the unfolding of triosephosphate isomerase: the monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica
Biochemistry
46
8624-8633
2007
Saccharomyces cerevisiae, Entamoeba histolytica
Najera, H.; Dagdug, L.; Fernandez-Velasco, D.A.
Thermodynamic and kinetic characterization of the association of triosephosphate isomerase: The role of diffusion
Biochim. Biophys. Acta
1774
985-994
2007
Saccharomyces cerevisiae
Gonzalez-Mondragon, E.; Zubillaga, R.A.; Hernandez-Arana, A.
Effect of a specific inhibitor on the unfolding and refolding kinetics of dimeric triosephosphate isomerase: establishing the dimeric and similarly structured nature of the main transition states on the forward and backward reactions
Biophys. Chem.
125
172-178
2007
Saccharomyces cerevisiae
Rozovsky, S.; McDermott, A.E.
Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
Proc. Natl. Acad. Sci. USA
104
2080-2085
2007
Saccharomyces cerevisiae
Peimbert, M.; Dominguez-Ramirez, L.; Fernandez-Velasco, D.A.
Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution
Biochemistry
47
5556-5564
2008
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae
Reyes-Lopez, C.A.; Gonzalez-Mondragon, E.; Benitez-Cardoza, C.G.; Chanez-Cardenas, M.E.; Cabrera, N.; Perez-Montfort, R.; Hernandez-Arana, A.
The conserved salt bridge linking two C-terminal beta /alpha units in homodimeric triosephosphate isomerase determines the folding rate of the monomer
Proteins Struct. Funct. Bioinform.
72
972-979
2008
Saccharomyces cerevisiae
Xu, Y.; Lorieau, J.; McDermott, A.E.
Triosephosphate isomerase: 15N and 13C chemical shift assignments and conformational change upon ligand binding by magic-angle spinning solid-state NMR spectroscopy
J. Mol. Biol.
397
233-248
2010
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae
Go, M.K.; Koudelka, A.; Amyes, T.L.; Richard, J.P.
The role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach
Biochemistry
49
5377-5389
2010
Saccharomyces cerevisiae
Wierenga, R.K.; Kapetaniou, E.G.; Venkatesan, R.
Triosephosphate isomerase: a highly evolved biocatalyst
Cell. Mol. Life Sci.
67
3961-3982
2010
Entamoeba histolytica (O02611), Oryctolagus cuniculus (P00939), Gallus gallus (P00940), Saccharomyces cerevisiae (P00942), Geobacillus stearothermophilus (P00943), Trypanosoma brucei brucei (P04789), Escherichia coli (P0A858), Giardia intestinalis (P36186), Thermotoga maritima (P36204), Leishmania mexicana (P48499), Moritella marina (P50921), Trypanosoma cruzi (P52270), Helicobacter pylori (P56076), Homo sapiens (P60174), Pyrococcus woesei (P62003), Mycobacterium tuberculosis (P9WG43), Plasmodium falciparum (Q07412), Caenorhabditis elegans (Q10657), Methanocaldococcus jannaschii (Q58923), Bartonella henselae (Q8L1Z5), Tenebrio molitor (Q8MPF2), Thermoproteus tenax (Q8NKN9), Mycobacterium tuberculosis H37Rv (P9WG43)
Sullivan, B.J.; Durani, V.; Magliery, T.J.
Triosephosphate isomerase by consensus design: dramatic differences in physical properties and activity of related variants
J. Mol. Biol.
413
195-208
2011
Saccharomyces cerevisiae
Aqvist, J.
Cold adaptation of triosephosphate isomerase
Biochemistry
56
4169-4176
2017
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae, Moritella marina (P50921), Moritella marina, Saccharomyces cerevisiae 288c (P00942)
Labastida-Polito, A.; Garza-Ramos, G.; Camarillo-Cadena, M.; Zubillaga, R.; Hernández-Arana, A.
Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase
BMC Biochem.
16
20
2015
Saccharomyces cerevisiae
Zhai, X.; Amyes, T.L.; Richard, J.P.
Role of loop-clamping side chains in catalysis by triosephosphate isomerase
J. Am. Chem. Soc.
137
15185-15197
2015
Saccharomyces cerevisiae (P00942)
Kulkarni, Y.S.; Liao, Q.; Petrovi?, D.; Krueger, D.M.; Strodel, B.; Amyes, T.L.; Richard, J.P.; Kamerlin, S.C.L.
Enzyme architecture Modeling the operation of a hydrophobic clamp in catalysis by triosephosphate isomerase
J. Am. Chem. Soc.
139
10514-10525
2017
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae 288c (P00942)
Kulkarni, Y.S.; Liao, Q.; Bylehn, F.; Amyes, T.L.; Richard, J.P.; Kamerlin, S.C.L.
Role of ligand-driven conformational changes in enzyme catalysis Modeling the reactivity of the catalytic cage of triosephosphate isomerase
J. Am. Chem. Soc.
140
3854-3857
2018
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae 288c (P00942)
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