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5.3.1.1: triose-phosphate isomerase

This is an abbreviated version!
For detailed information about triose-phosphate isomerase, go to the full flat file.

Word Map on EC 5.3.1.1

Reaction

D-glyceraldehyde 3-phosphate
=
glycerone phosphate

Synonyms

CP 25, CTIMC, cTPI, cytoplasmic TPI, cytoplasmic triosephosphate isomerase, cytoTPI, D-glyceraldehyde-3-phosphate ketol-isomerase, GlTIM, Isomerase, triose phosphate, Lactacin B inducer protein, monoTIM, PfTIM, PfuTIM, Phosphotriose isomerase, plastidic TPI, plastidic triosephosphate isomerase, pTPI, SSO2592, TcTIM, TIM, TIM1, TIM2, TonTIM, TpI, TPI1, TpiA, Triose phosphate isomerase, Triose phosphate mutase, Triose phosphoisomerase, Triosephosphate isomerase, Triosephosphate mutase, vTIM

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.1 triose-phosphate isomerase

Renatured

Renatured on EC 5.3.1.1 - triose-phosphate isomerase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibitor 2-phosphoglycolate brings about a large decrease in the unfolding rate constant of the protein. Thermodynamics of binding reveal a dimeric transition state
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protein unfolded in 3.2 M guanidinium-HCl is diluted to final concentrations of 0.32 M guanidinium-HCl, 16% recovery of wild-type enzyme after 72 h, 2.1-2.6% recovery of the mutant enzymes D227N, D227A, R191S and R191A after 72 h
renaturation into catalytic active enzyme by removal of the dissociating agent
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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
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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
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study on thermal dissociation and unfolding of enzyme and a monomeric variant obtained by chemical derivatization. During wild-type unfolding, sequential transitions corresponding to dimer dissociation into a compact monomeric intermediate followed by unfolding and further aggregation of the intermediate occurr. In the case of the monomeric variant, a single transition, analogous to the second transition of wild-type, is observed. Dimer dissociation is not restricted to localized interface reorganization. Dissociation represents 55% of the total enthalpy change. Subunit assembly is probably best represented by a fly-casting mechanism
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
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study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Saccharomyces cerevisiae. 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
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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
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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
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
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two conformational isomers of the enzyme that exhibit significantly different stabilities and kinetics of unfolding. Complete unfolding of the two isolated conformers at a 1.5 M guanidine-HCl followed by refolding by removal of the denaturant completely abolishes the differences in their unfolding kinetics
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unfolding of triosephosphate isomerase in urea is highly cooperative, and no folding intermediate is detected. The thermodynamic parameters just reflect the unfolding of dissociated folded monomer to fully unfolded monomer transition. Unfolding follows an irreversible two-state step with a slow aggregation process. The two subunits of the active enzyme unfold independently
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unfolding/refolding reactions of monomeric enzyme evaluated using the two-state model