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D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
dihydroxyacetone 3-phosphate
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
glycerone phosphate
D-glyceraldehyde 3-phosphate
glycerone phosphate
methylglyoxal + phosphate
-
-
-
?
additional information
?
-
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
isomerization of D-glyceraldehyde 3-phosphate in D2O proceeds with 49% intramolecular transfer of the 1 H label from substrate to product dihydroxyacetone phosphate
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
the active site of free enzyme, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
cytoplasmic triosephosphate isomerase may be important in the glycolytic pathway for the supply of C to respiratory and biosynthetic pathways during active growth
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
stereospecific reaction via an enzyme-bound enediol(ate) intermediate, proton transfer from D-glyceraldehyde 3-phosphate to the carboxylate side chain of TIM Glu165, irreversible labeling with deuterium , overview
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
the reaction is essential in vivo
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
triosephosphate isomerase is an enolizing enzyme, which catalyses the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
TIM is highly specific for the substrates
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone 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
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
key reaction in glycolysis
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
r
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
-
-
?
dihydroxyacetone 3-phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
r
dihydroxyacetone 3-phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
r
glycerone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
glycerone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
?
glycerone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
?
glycerone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
glycerone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
?
glycolaldehyde
?
-
-
-
-
?
glycolaldehyde
?
-
TIM-catalyzed reactions of glycolaldehyde are activated by phosphite dianion, kinetics, overview
-
-
?
glycolaldehyde
?
-
-
-
-
?
additional information
?
-
enzyme is confirmed by total proteome analysis of glycerol-grown cells
-
-
?
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
?
additional information
?
-
the proton transfer reaction from PGH to the Glu167 side chain, when PGH becomes sequestered in the active site, active site modeling, overview
-
-
?
additional information
?
-
-
Tau, main component of the aberrant paired helical filaments found in Alzheimer's disease, interacts with the enzyme and protects TPI against oxidative damage, overview. Interaction between Tau and triose phosphate isomerase occurs in a normal, nondisease state as well as in a neurodegeneration state
-
-
?
additional information
?
-
-
formation of a two-part substrate by carving up D-glyceraldehyde 3-phosphate into the minimal neutral two-carbon sugar glycolaldehyde and phosphite dianion pieces. Enzyme catalyzes proton transfer from glycolaldehyde in D2O with a ratio of kcat to Km of 0.26 per M and s. Addition of exogenous phosphite dianion results in a large increase in the observed second-order rate constant for turnover of glycolaldehyde. Binding of phosphite dianion to the free enzyme is 700fold weaker than its binding to the fleeting complex of the enzyme with the altered substrate in the transition state
-
-
?
additional information
?
-
importance of conserved residues in the vicinity of the active site that serve to position the functional K12 residue. A network of key interactions spans the interacting subunits
-
-
?
additional information
?
-
-
importance of conserved residues in the vicinity of the active site that serve to position the functional K12 residue. A network of key interactions spans the interacting subunits
-
-
?
additional information
?
-
Plasmodium falciparum TIM is unique in possessing a Phe residue at position 96 in place of the conserved Ser that is found in TIMs from the majority of other organisms
-
-
?
additional information
?
-
-
Plasmodium falciparum TIM is unique in possessing a Phe residue at position 96 in place of the conserved Ser that is found in TIMs from the majority of other organisms
-
-
?
additional information
?
-
enzyme is involved in arsenate reduction
-
-
?
additional information
?
-
-
enzyme is involved in arsenate reduction
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(1E,3E,6E,8E)-1,9-di(furan-2-yl)nona-1,3,6,8-tetraen-5-one
-
compound binds to the dimer interface and is unable to inactivate Trypanosoma brucei TIM or Homo sapiens TIM at concentrations higher than 100 microM. Compound also affects cruzipain
(1Z,2Z)-N,N'-dihydroxy-4-methylcyclohexa-3,5-diene-1,2-diimine
-
-
(2E)-2-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarbothioamide
-
irreversible inhibitor
(2E)-2-[2-[(3-oxido-2,1,3-benzoxadiazol-5-yl)methoxy]benzylidene]-N-(prop-2-en-1-yl)hydrazinecarbothioamide
-
irreversible inhibitor
(2E)-N-(naphthalen-2-yl)-2-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]hydrazinecarboxamide
-
irreversible inhibitor
(2E)-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarboxamide
-
irreversible inhibitor
(2E,5E)-2,5-bis[(2E)-3-(thiophen-2-yl)prop-2-en-1-ylidene]cyclopentan-1-one
-
compound is unable to inactivate Trypanosoma brucei TIM or Homo sapiens TIM at concentrations higher than 100 microM. Compound also affects cruzipain
(2E,6E)-2,6-bis[(2E)-3-(furan-2-yl)prop-2-en-1-ylidene]cyclohexan-1-one
-
compound binds to the dimer interface and is unable to inactivate Trypanosoma brucei TIM or Homo sapiens TIM at concentrations higher than 100 microM. Compound also affects cruzipain
(4-methyl-1,2,3-thiadiazol-5-yl)methanol
-
29% inhibition at 0.4 mM
1,2,6-thiadiazine
-
irreversible inhibitor
1-Chloro-3-hydroxyacetone
-
-
2,2'-methylenebis(1,3-benzothiazole)
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor
2,9-dimethyl-beta-carbolinium ion
-
-
2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
-
2-carboxyethyl methanethiosulfonate
modifies four Cys per subunit of dimeric protein and induces 97% of inactivation. Inactivation does not affect secondary structure nor induce dimer dissociation. Cys modification decreases thermal stability of the enzyme
2-carboxyethylphosphonic acid
-
-
2-methyl-beta-carbolinium ion
-
-
2-phenyl-4H-chromen-4-one
-
-
2-phosphoglycolic acid
-
-
2-[(1E)-2-nitroprop-1-en-1-yl]thiophene
-
-
2-[(3-aminophenyl)disulfanyl]aniline
-
-
3,5-diphenyl-1,2,4-thiadiazole
-
74% inhibition at 0.4 mM
3-(2-benzothiazolylthio)-1-propanesulfonic acid
binds to the dimer interface of the enzyme and thereby abolishes its function with a high level of selectivity
3-(4-methylphenyl)-5-[(4-methylphenyl)sulfonyl]-1,2,4-thiadiazole
-
-
3-nitrobiphenyl-4-amine
-
-
4-(4-nitrobenzylidene)-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor, 85% inhibition at 0.4 mM
4-[(5-nitrofuran-2-yl)methylidene]-4H-1,2,6-thiadiazine-3,5-diamine 1,1-dioxide
-
irreversible inhibitor
4-[(5-nitrothiophen-2-yl)methylidene]-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor
5,5'-dithio-bis(2-nitrobenzoic acid)
5,5'-dithiobis(2-nitrobenzoate)
5-[(1E)-2-nitroprop-1-en-1-yl]-1,3-benzodioxole
-
-
6,6'-bi-1,3-benzothiazole-2,2'-diamine
6-phosphogluconate
-
5 mM, 9% inhibition
6-[(E)-2-(5-nitrothiophen-2-yl)ethenyl]-2,1,3-benzoxadiazole 1-oxide
-
irreversible inhibitor
6-[(E)-2-[(4-fluorophenyl)sulfanyl]ethenyl]-2,1,3-benzoxadiazole 1-oxide
-
irreversible inhibitor
8-bromo-5,10-dioxidophenazin-2-yl chloroacetate
-
50% inhibition at 0.4 mM
Atrazine
-
a herbicide which interferes with photosynthesis
bromohydroxyacetone phosphate
butylbrevifolin carboxylate
-
-
Chloroacetol phosphate
-
-
citrate
-
25 mM, 9% inhibition
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
cyclo[Trp-Tyr(OSO3Na)-D-Phe-Thr(OSO3Na)-Lys(benzyloxycarbonyl)-]
-
noncompetitive, reversible
D-erythrose 4-phosphate
-
-
Diamide
1 mM, presence of glutathione, complete inhibition by S-glutathionylation
ethyl 3-(3,5-di-tert-butyl-4-hydroxyphenyl)-1,2,4-thiadiazole-5-carboxylate
-
-
ethyl 3-phenyl-1,2,4-thiadiazole-5-carboxylate
-
-
ethylbrevifolin carboxylate
-
-
fluorodifen
-
a herbicide which interferes with photosynthesis
fructose 1,6-diphosphate
-
5 mM, 69% inhibition
fructose 6-phosphate
-
5 mM, 44% inhibition
glucose 1-phosphate
-
5 mM, 10% inhibition
glucose 6-phosphate
-
5 mM, 25% inhibition
glutathione disulfide
modification of residues Cys127 and Cys218
GSSG
-
oxidized glutathione is a strong inhibitor of the enzyme at low concentrations
KFGNGSYTGEVS
peptide that corresponds to loop 3 of the triosephosphate isomerase, residues 68-79. Efficient inhibitor with the activity falling to about 45% at 1000fold molar excess of the peptide in case of the wild-type enzyme. In the case of either of the mutants, Y74C and Y74G, even at 100fold molar excess of the peptide, only 30% activity can be obtained
KYGNGSCTGEVS
peptide that is an analog of the peptide that corresponds to loop 3 of the protein, residues 68-79, with the replacement Y74C and F69Y. Inhibits the activity of the mutant enzymes Y74C and Y74G, with about 40% activity remaining in the presence of 1000fold molar excess of the peptide
Mannotriose
-
docking simulation
methyl methanethiosulfonate
methylbrevifolin carboxylate
-
molecular docking simulations and enzyme binding structure, and inhibition kinetics, overview
methylmethane thiosulfonate
N-[(2-oxido-4-phenyl-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
-
72% inhibition at 0.4 mM
N-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
-
41% inhibition at 0.4 mM
phenazine 5,9-dioxide
-
84% inhibition at 0.4 mM
phosphoglycoloaldoxime
-
-
phosphoglycolohydrazide
-
-
Phosphoglycolohydroxamate
S-Phenyl-p-toluenethiosulfonate
succinate
-
5 mM, 9% inhibition
[3-amino-3-(hydroxyimino)propyl]phosphonic acid
-
-
1,2,4-thiadiazole
-
59% inhibition at 0.1 mM
2,2'-methylenebis(1,3-benzothiazole)
-
irreversible inactivation
2,2'-methylenebis(1,3-benzothiazole)
-
irreversible inactivation
2,2'-methylenebis(1,3-benzothiazole)
-
40% inactivation at 0.05 mM, irreversible
2,4-dinitrofluorobenzene
-
-
2,4-dinitrofluorobenzene
-
no inhibition
2-Phosphoglycolate
-
-
2-Phosphoglycolate
-
competitive inhibition
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
2-Phosphoglycolate
-
competitive inhibition
2-Phosphoglycolate
-
competitive inhibition
3-phosphoglycerate
-
-
3-phosphoglycerate
binding at the active site with the dimer-interface site showing strong electrostatic anchoring of the phosphate group involving the Arg98 and Lys112 residues of TIM, comparisons of binding structures at the interface, overview
4,4'-Dithiopyridine
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
derivatizes four of the five Cys per subunit of dimeric protein, resulting in inactivation and dissociation of the dimer to stable monomers
5,5'-dithio-bis(2-nitrobenzoic acid)
about 50% inhibition at about 0.05 mM
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
no inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
irreversible inactivation. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
irreversible inactivation. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
91% inactivation at 0.05 mM, irreversible. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
-
Acetylphosphate
-
-
Acetylphosphate
-
competitive
arsenate
-
-
arsenate
-
competitive inhibition
arsenate
-
competitive inhibition
AsO2-
-
-
AsO43-
-
competitive
ATP
-
-
ATP
-
5 mM, 39% inhibition
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
bromohydroxyacetone phosphate
suicide inhibitor
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
-
no inhibition
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
-
no inhibition
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
-
no inhibition
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
-
-
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
-
no inhibition
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
-
no inhibition
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
-
no inhibition
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
-
-
D-alpha-glycerophosphate
-
competitive
D-alpha-glycerophosphate
-
-
D-alpha-glycerophosphate
-
competitive
D-alpha-glycerophosphate
-
competitive
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
H2O2
0.5 mM, 120 min, 30% loss of activity in presence and absence of glutathione
H2O2
the inhibition of the enzyme is negligible when incubated with 0.1 mM H2O2, whereas a 10% inhibition is observed with 1 mM H2O2
iodoacetate
-
-
iodoacetate
-
no inhibition
methyl methanethiosulfonate
-
no inhibition
methyl methanethiosulfonate
derivatizes three of the five Cys per subunit of dimeric protein and induces 50% of inactivation. Inactivation does not affect secondary structure nor induce dimer dissociation. Cys modification decreases thermal stability of the enzyme
methyl methanethiosulfonate
-
the sensitivity of enzyme from Trypanosoma cruzi is about 40times higher than that of Trypanosoma brucei and 200times higher than that of Leishmania mexicana
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
about 50% inhibition at about 0.05 mM
methyl methanethiosulfonate
-
no inhibition
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
derivatizes Cys14 to a methyl sulfide
methyl methanethiosulfonate
-
the sensitivity of enzyme from Trypanosoma cruzi is about 40times higher than that of Trypanosoma brucei and 200times higher than that of Leishmania mexicana
methyl methanethiosulfonate
-
the sensitivity of enzyme from Trypanosoma cruzi is about 40times higher than that of Trypanosoma brucei and 200times higher than that of Leishmania mexicana
methylmethane thiosulfonate
-
0.6 mM, 2 h, complete loss of activity, dissociates the dimeric enzyme inducing formation of a compact monomeric state
methylmethane thiosulfonate
-
induces 75% enzyme inactivation within 15 min at 0.25 mM concentration
methylmethane thiosulfonate
-
modification at C15 in the dimer interface, inducing abolition of catalysis and structural changes. Susceptibility of Trypanosoma cruzi enzyme to modification of C15 is nearly 100fold higher than susceptibility of C15 of Trypanosoma brucei
methylmethane thiosulfonate
-
60% residual activity at 0.1 mM
methylmethane thiosulfonate
inactivation by sulfhydroxylation
methylmethane thiosulfonate
-
modification at C15 in the dimer interface, inducing abolition of catalysis and structural changes. Susceptibility of Trypanosoma cruzi enzyme to modification of C15 is nearly 100fold higher than susceptibility of C15 of Trypanosoma brucei
methylmethane thiosulfonate
-
almost complete inhibition at 0.1 mM
methylmethane thiosulfonate
inactivation by sulfhydroxylation
N-ethylmaleimide
0.5 mM, 60 min, more than 90% loss of activity. Addition of dithiothreitol does not restore activity. In the presence of 1 mM glutathione, the addition of 0.5 mM N-ethylmaleimide does not significantly affect activity
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
PCMB
-
-
phosphate
competitive, occupies the substrate binding pocket
phosphoenolpyruvate
-
competitive
phosphoenolpyruvate
competitive
phosphoenolpyruvate
-
competitive
Phosphoglycolate
-
Phosphoglycolate
-
2-phosphoglycolate
Phosphoglycolate
-
competitive
Phosphoglycolate
-
2-phosphoglycolate
Phosphoglycolate
-
and its corresponding hydroxamate; competitive
Phosphoglycolate
-
competitive
Phosphoglycolate
-
2-phosphoglycolate
Phosphoglycolohydroxamate
the reaction-intermediate analogue binds to the active site with two hydrogen-bonding interactions between PGH and the Glu167 side-chain oxygen atoms
Phosphoglycolohydroxamate
-
-
Phosphoglycolohydroxamate
-
-
S-Phenyl-p-toluenethiosulfonate
-
no inhibition
S-Phenyl-p-toluenethiosulfonate
-
-
S-Phenyl-p-toluenethiosulfonate
-
-
S-Phenyl-p-toluenethiosulfonate
-
no inhibition
S-Phenyl-p-toluenethiosulfonate
-
-
SO42-
-
CuSO4
additional information
-
in drug-resistant SGC7901 cells induced by vincristine sulfate, triosephosphate isomerase is downregulated.The sensitivity of TPI-SGC7901/VCR cells to adriamycin, vincristine, 5-fluorouracil and cis-dichlorodiamine platinum, as well as the accumulation and retention to adriamycin, are significantly increased when compared to their control cell lines
-
additional information
-
TPI phosphorylation by cyclin A/Cdk2 kinase leads to reduced TPI activity, prevented by treatment with olomoucine, a specific inhibitor of Cdk2
-
additional information
-
not inhibited by 1,2,6-thiadiazine, phenazine 5,9-dioxide, and 1,3,4-oxathiazole
-
additional information
-
recombinant expression of Tau in CHO-K1 cells leads to increased protection of TPI against oxidative damage, but also to decreased enzyme activity, with unaltered TPI expression levels
-
additional information
ANWKCNGTLE, the peptide that corresponds to loop 1 of triosephosphate isomerase, residues 9-18, shows only negligible inhibition of wild-type enzyme and mutant enzymes Y74G and Y74C, with a fall in the enzymatic activity by only about 20% at 1000fold molar excess of the peptide
-
additional information
-
ANWKCNGTLE, the peptide that corresponds to loop 1 of triosephosphate isomerase, residues 9-18, shows only negligible inhibition of wild-type enzyme and mutant enzymes Y74G and Y74C, with a fall in the enzymatic activity by only about 20% at 1000fold molar excess of the peptide
-
additional information
-
stronger inhibition by alpha-(1,3)-mannooligosaccharides than with triose, binding constants, overview
-
additional information
-
brevifolin carboxylate derivatives isolated from Geranium bellum selectively inactivate the enzyme partially, no inhibition by methyl tri-O-methylbrevifolin carboxylate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.00004 - 50
D-glyceraldehyde 3-phosphate
0.59 - 25
dihydroxyacetone 3-phosphate
0.0025 - 18
dihydroxyacetone phosphate
0.26 - 2.5
glycerone phosphate
additional information
additional information
-
-
-
0.00004
D-glyceraldehyde 3-phosphate
mutant V167P/W168E, pH 7.5, 25°C
0.084
D-glyceraldehyde 3-phosphate
-
22°C, pH 7.6
0.091
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.14
D-glyceraldehyde 3-phosphate
-
mutant C14S/A73C, 25°C, pH 7.4
0.14
D-glyceraldehyde 3-phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
0.16
D-glyceraldehyde 3-phosphate
mutant P168A, 25°C, pH 7.6
0.18
D-glyceraldehyde 3-phosphate
-
mutant E168D, pH 7.4, 25°C
0.19
D-glyceraldehyde 3-phosphate
-
recombinant wild-type enzyme
0.2
D-glyceraldehyde 3-phosphate
-
active form P2 of TIM, at 25°C, pH 7.4
0.21
D-glyceraldehyde 3-phosphate
pH 8.0, 90°C
0.21
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
0.22
D-glyceraldehyde 3-phosphate
-
plastidic triosephosphate isomerase
0.23
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
0.23
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
0.24
D-glyceraldehyde 3-phosphate
mutant enzyme S227A
0.245
D-glyceraldehyde 3-phosphate
pH 6.5, 70°C
0.25
D-glyceraldehyde 3-phosphate
wild-type enzyme
0.25
D-glyceraldehyde 3-phosphate
-
D-glyceraldehyde 3-phosphate
0.25
D-glyceraldehyde 3-phosphate
-
isoenzyme A
0.25
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
0.25
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
0.25
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.26
D-glyceraldehyde 3-phosphate
wild-type, pH 7.6, 25°C
0.26
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH 7.6
0.27
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.28
D-glyceraldehyde 3-phosphate
mutant enzyme S227N
0.28
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C
0.28
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C
0.28
D-glyceraldehyde 3-phosphate
mutant W162F
0.29
D-glyceraldehyde 3-phosphate
-
cytoplasmic triosephosphate isomerase
0.29
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
0.29
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.3
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
0.3
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
0.3
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126S
0.3
D-glyceraldehyde 3-phosphate
-
active form P1 of TIM, at 25°C, pH 7.4
0.3
D-glyceraldehyde 3-phosphate
mutant I45V, pH 7.4, 25°C
0.303
D-glyceraldehyde 3-phosphate
-
mutant I170T, pH not specified in the publication, temperature not specified in the publication
0.31
D-glyceraldehyde 3-phosphate
-
-
0.31
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C
0.31
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C
0.31
D-glyceraldehyde 3-phosphate
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.32
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14T
0.32
D-glyceraldehyde 3-phosphate
mutant I45L, pH 7.4, 25°C
0.328
D-glyceraldehyde 3-phosphate
-
in 50 mM Tris, pH 7.6, at 25°C
0.33
D-glyceraldehyde 3-phosphate
-
isoenzyme B
0.33
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14P
0.33
D-glyceraldehyde 3-phosphate
pH 7.6, mutant enzyme Y74C
0.34
D-glyceraldehyde 3-phosphate
-
enzyme form I
0.34
D-glyceraldehyde 3-phosphate
mutant enzyme R191S
0.34
D-glyceraldehyde 3-phosphate
pH 7.6, mutant enzyme Y74G
0.35
D-glyceraldehyde 3-phosphate
-
0.35
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, wild-type enzyme
0.35
D-glyceraldehyde 3-phosphate
pH 7.6, wild-type enzyme
0.35
D-glyceraldehyde 3-phosphate
-
mutant C14S/S71C, 25°C, pH 7.4
0.35
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
0.35
D-glyceraldehyde 3-phosphate
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
0.35
D-glyceraldehyde 3-phosphate
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.35
D-glyceraldehyde 3-phosphate
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25°C
0.38
D-glyceraldehyde 3-phosphate
-
wild-type, 25°C, pH 7.4
0.39
D-glyceraldehyde 3-phosphate
pH 7.6, wild-type enzyme
0.39
D-glyceraldehyde 3-phosphate
mutant I45A, pH 7.4, 25°C
0.39
D-glyceraldehyde 3-phosphate
mutant lacking loop 3, pH 7.4, 25°C
0.4
D-glyceraldehyde 3-phosphate
-
-
0.4067
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
0.42
D-glyceraldehyde 3-phosphate
-
-
0.42
D-glyceraldehyde 3-phosphate
-
-
0.42
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14V
0.42
D-glyceraldehyde 3-phosphate
-
mutant C15A, pH 7.4, 25°C
0.42
D-glyceraldehyde 3-phosphate
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.43
D-glyceraldehyde 3-phosphate
-
enzyme form II
0.43
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14A
0.43
D-glyceraldehyde 3-phosphate
mutant W196F
0.43
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
0.44
D-glyceraldehyde 3-phosphate
-
-
0.44
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
0.45
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25°C
0.45
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
0.45
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
0.46
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25°C
0.47
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, wild-type enzyme
0.47
D-glyceraldehyde 3-phosphate
in 100 mM triethanolamine, pH 7.4, at 25°C
0.48
D-glyceraldehyde 3-phosphate
-
mutant C14S/S79C, 25°C, pH 7.4
0.48
D-glyceraldehyde 3-phosphate
mutant C127S, pH 7.8, 30°C
0.5
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14S
0.5
D-glyceraldehyde 3-phosphate
-
mutant C14S, 25°C, pH 7.4
0.5
D-glyceraldehyde 3-phosphate
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C
0.5
D-glyceraldehyde 3-phosphate
mutant C127S/C218S, pH 7.8, 30°C
0.5
D-glyceraldehyde 3-phosphate
mutant lacking loop 3, pH 7.4, 25°C
0.51
D-glyceraldehyde 3-phosphate
mutant V45A, pH 7.4, 25°C
0.52
D-glyceraldehyde 3-phosphate
mutant I45F, pH 7.4, 25°C
0.53
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, dimeric enzyme form
0.55
D-glyceraldehyde 3-phosphate
-
enzyme form III
0.6
D-glyceraldehyde 3-phosphate
-
cytosolic enzyme
0.6
D-glyceraldehyde 3-phosphate
-
D-glyceraldehyde 3-phosphate
0.6
D-glyceraldehyde 3-phosphate
mutant F12W
0.61
D-glyceraldehyde 3-phosphate
mutant A178L, pH 7.6, 25°C
0.62
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
0.62
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
0.62
D-glyceraldehyde 3-phosphate
wild-type, pH 7.6, 23°C
0.68
D-glyceraldehyde 3-phosphate
-
chloroplastic enzyme
0.68
D-glyceraldehyde 3-phosphate
pH 8.0, 90°C
0.687
D-glyceraldehyde 3-phosphate
-
mutant I170V, pH not specified in the publication, temperature not specified in the publication
0.69
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C
0.69
D-glyceraldehyde 3-phosphate
-
mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C
0.7
D-glyceraldehyde 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
0.73
D-glyceraldehyde 3-phosphate
mutant W75F/W162F/W196F
0.74
D-glyceraldehyde 3-phosphate
mutant W75F
0.75
D-glyceraldehyde 3-phosphate
-
mutant C14S/A69C, 25°C, pH 7.4
0.78
D-glyceraldehyde 3-phosphate
wildtype
0.8
D-glyceraldehyde 3-phosphate
-
0.8
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126A
0.8
D-glyceraldehyde 3-phosphate
mutant T75S, pH 7.6, 23°C
0.84
D-glyceraldehyde 3-phosphate
pH 7.0, 25°C
0.86
D-glyceraldehyde 3-phosphate
mutant T75N, pH 7.6, 23°C
0.87
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, tetrameric enzyme form
0.87
D-glyceraldehyde 3-phosphate
mutant F96A, 25°C, pH not specified in the publication
0.9
D-glyceraldehyde 3-phosphate
-
-
0.9
D-glyceraldehyde 3-phosphate
-
-
0.91
D-glyceraldehyde 3-phosphate
-
mutant D225Q, pH 7.4, 25°C
0.91
D-glyceraldehyde 3-phosphate
mutant T75V, pH 7.6, 23°C
0.94
D-glyceraldehyde 3-phosphate
mutant W173F
0.97
D-glyceraldehyde 3-phosphate
presence of methyl methanethiosulfonate
1
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
1
D-glyceraldehyde 3-phosphate
mutant W162F/W173F/W196F
1
D-glyceraldehyde 3-phosphate
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.02
D-glyceraldehyde 3-phosphate
mutant F96S/L167V, 25°C, pH not specified in the publication
1.03
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
1.09
D-glyceraldehyde 3-phosphate
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C
1.1
D-glyceraldehyde 3-phosphate
mutant enzyme R191A
1.1
D-glyceraldehyde 3-phosphate
-
25°C, pH 7., wild-type enzyme
1.1
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
1.12
D-glyceraldehyde 3-phosphate
mutant W75F/W162F/W173F
1.13
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25°C
1.15
D-glyceraldehyde 3-phosphate
mutant T75C, pH 7.6, 23°C
1.2
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
1.2
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G
1.2
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C
1.2
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96W
1.2
D-glyceraldehyde 3-phosphate
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.2
D-glyceraldehyde 3-phosphate
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C
1.2
D-glyceraldehyde 3-phosphate
mutant F96S/S73A, 25°C, pH not specified in the publication
1.26
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C
1.27
D-glyceraldehyde 3-phosphate
-
-
1.29
D-glyceraldehyde 3-phosphate
mutant I45Y, pH 7.4, 25°C
1.32
D-glyceraldehyde 3-phosphate
wild-type, pH 7.8, 30°C
1.373
D-glyceraldehyde 3-phosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
1.4
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
1.4
D-glyceraldehyde 3-phosphate
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.5
D-glyceraldehyde 3-phosphate
-
at pH 7.5 and 37°C
1.5
D-glyceraldehyde 3-phosphate
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.5
D-glyceraldehyde 3-phosphate
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.67
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
1.68
D-glyceraldehyde 3-phosphate
mutant C218S, pH 7.8, 30°C
1.78
D-glyceraldehyde 3-phosphate
mutant I45G, pH 7.4, 25°C
1.8
D-glyceraldehyde 3-phosphate
mutant S211G, pH 7.5, 25°C
1.85
D-glyceraldehyde 3-phosphate
mutant F96Y, 25°C, pH not specified in the publication
1.9
D-glyceraldehyde 3-phosphate
-
wild-type enzyme
1.9
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
1.9
D-glyceraldehyde 3-phosphate
mutant W75F/W173F/W196F
2.18
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96S
2.2
D-glyceraldehyde 3-phosphate
mutant F96S, 25°C, pH not specified in the publication
2.4
D-glyceraldehyde 3-phosphate
mutant Y208F, pH 7.5, 25°C
2.44
D-glyceraldehyde 3-phosphate
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C
2.49
D-glyceraldehyde 3-phosphate
mutant D213A, pH 7.5, 25°C
2.49
D-glyceraldehyde 3-phosphate
-
mutant D213A, pH 7.5, 25°C
2.62
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96H
2.9
D-glyceraldehyde 3-phosphate
mutant Y208A, pH 7.5, 25°C
3.04
D-glyceraldehyde 3-phosphate
in 100 mM triethanolamine (pH 7.4), at 25°C
3.27
D-glyceraldehyde 3-phosphate
mutant D213Q, pH 7.5, 25°C
3.27
D-glyceraldehyde 3-phosphate
-
mutant D213Q, pH 7.5, 25°C
3.3
D-glyceraldehyde 3-phosphate
monomeric mutant A178L, pH 7.6, 25°C
3.4
D-glyceraldehyde 3-phosphate
mutant Y208T, pH 7.5, 25°C
3.46
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
3.46
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.5, 25°C
3.56
D-glyceraldehyde 3-phosphate
mutant K183S, pH 7.5, 25°C
3.56
D-glyceraldehyde 3-phosphate
-
mutant K183S, pH 7.5, 25°C
3.6
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14F
3.7
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme K174G/T175G/A176G
3.8
D-glyceraldehyde 3-phosphate
monomeric wild-type, pH 7.6, 25°C
3.9
D-glyceraldehyde 3-phosphate
mutant Y208S, pH 7.5, 25°C
4
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
4.8
D-glyceraldehyde 3-phosphate
-
mutant A238S
4.8
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme A238S
8.6
D-glyceraldehyde 3-phosphate
presence of 2-carboxyethyl methanethiosulfonate
9.09
D-glyceraldehyde 3-phosphate
mutant K183A, pH 7.5, 25°C
9.09
D-glyceraldehyde 3-phosphate
-
mutant K183A, pH 7.5, 25°C
12
D-glyceraldehyde 3-phosphate
mutant S211A, pH 7.5, 25°C
50
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
0.59
dihydroxyacetone 3-phosphate
wild-type, pH 7.5, 25°C
1.7
dihydroxyacetone 3-phosphate
wild-type, pH 7.5, 25°C
2.3
dihydroxyacetone 3-phosphate
-
at pH 7.5 and 37°C
3.2
dihydroxyacetone 3-phosphate
mutant S211G, pH 7.5, 25°C
4
dihydroxyacetone 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
11
dihydroxyacetone 3-phosphate
mutant Y208T, pH 7.5, 25°C
17
dihydroxyacetone 3-phosphate
mutant Y208A, pH 7.5, 25°C
17
dihydroxyacetone 3-phosphate
mutant Y208F, pH 7.5, 25°C
25
dihydroxyacetone 3-phosphate
mutant Y208S, pH 7.5, 25°C
0.0025
dihydroxyacetone phosphate
in 100 mM Tris pH 7.8, at 25°C
0.077
dihydroxyacetone phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
0.49
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.5
dihydroxyacetone phosphate
mutant P168A, 25°C, pH 7.6
0.59
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.6
dihydroxyacetone phosphate
-
25°C, pH 7.4, mutant enzyme C126S
0.7
dihydroxyacetone phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
0.7
dihydroxyacetone phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
0.7
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.9
dihydroxyacetone phosphate
wild-type, pH 7.6, 25°C
0.9
dihydroxyacetone phosphate
wild-type, 25°C, pH 7.6
0.97
dihydroxyacetone phosphate
-
30°C, pH 7.6, wild-type enzyme
1.1
dihydroxyacetone phosphate
-
25°C, pH 7.4, dimeric enzyme form
1.4
dihydroxyacetone phosphate
mutant A178L, pH 7.6, 25°C
2.1
dihydroxyacetone phosphate
-
25°C, pH 7.4, wild-type enzyme
4
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
7.6
dihydroxyacetone phosphate
monomeric wild-type, pH 7.6, 25°C
9.3
dihydroxyacetone phosphate
monomeric mutant A178L, pH 7.6, 25°C
11
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G
15
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme K174G/T175G/A176G
18
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
0.26
glycerone phosphate
-
isoenzyme B
0.37
glycerone phosphate
-
isoenzyme A
0.59
glycerone phosphate
-
-
0.59
glycerone phosphate
-
-
0.67
glycerone phosphate
mutant enzyme R191A
0.69
glycerone phosphate
-
enzyme form III
0.7
glycerone phosphate
mutant enzyme D227N
0.75
glycerone phosphate
-
-
0.812
glycerone phosphate
pH 6.5, 70°C
0.82
glycerone phosphate
-
enzyme form II
0.88
glycerone phosphate
-
-
0.9
glycerone phosphate
mutant enzyme D227A
1
glycerone phosphate
wild-type enzyme
1.1
glycerone phosphate
-
recombinant wild-type enzyme
1.1
glycerone phosphate
-
glycerone phosphate
1.2
glycerone phosphate
-
-
1.23
glycerone phosphate
-
-
1.3
glycerone phosphate
-
recombinant enzyme
1.5
glycerone phosphate
-
enzyme form I
1.5
glycerone phosphate
-
glycerone phosphate, cytosolic enzyme
1.6
glycerone phosphate
mutant enzyme R191S
2.5
glycerone phosphate
-
chloroplastic enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.013 - 57500000
D-glyceraldehyde 3-phosphate
4.5 - 860
dihydroxyacetone 3-phosphate
0.06 - 800
dihydroxyacetone phosphate
63 - 1080
glycerone phosphate
additional information
additional information
-
0.013
D-glyceraldehyde 3-phosphate
mutant T75N, pH 7.6, 23°C
0.03
D-glyceraldehyde 3-phosphate
mutant 170-173del, pH 7.5, 25°C
0.034
D-glyceraldehyde 3-phosphate
mutant T75C, pH 7.6, 23°C
0.038
D-glyceraldehyde 3-phosphate
mutant T75S, pH 7.6, 23°C
0.038
D-glyceraldehyde 3-phosphate
mutant T75V, pH 7.6, 23°C
0.04
D-glyceraldehyde 3-phosphate
wild-type, pH 7.6, 23°C
0.25
D-glyceraldehyde 3-phosphate
monomeric mutant A178L, pH 7.6, 25°C
0.31
D-glyceraldehyde 3-phosphate
mutant lacking loop 3, pH 7.4, 25°C
0.6
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
0.69
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C
1
D-glyceraldehyde 3-phosphate
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C
1.04
D-glyceraldehyde 3-phosphate
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C
1.5
D-glyceraldehyde 3-phosphate
mutant lacking loop 3, pH 7.4, 25°C
1.7
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
1.9
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14F
2.2
D-glyceraldehyde 3-phosphate
monomeric wild-type, pH 7.6, 25°C
3.8
D-glyceraldehyde 3-phosphate
mutant F96A, 25°C, pH not specified in the publication
4
D-glyceraldehyde 3-phosphate
mutant F96S/L167V, 25°C, pH not specified in the publication
4.2
D-glyceraldehyde 3-phosphate
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C
4.3
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
4.6
D-glyceraldehyde 3-phosphate
mutant F96S/S73A, 25°C, pH not specified in the publication
5.5
D-glyceraldehyde 3-phosphate
mutant F96Y, 25°C, pH not specified in the publication
6.2
D-glyceraldehyde 3-phosphate
mutant F96S, 25°C, pH not specified in the publication
11
D-glyceraldehyde 3-phosphate
-
mutant E168D, pH 7.4, 25°C
13
D-glyceraldehyde 3-phosphate
mutant Y208F, pH 7.5, 25°C
14.8
D-glyceraldehyde 3-phosphate
mutant C127S/C218S, pH 7.8, 30°C
15.7
D-glyceraldehyde 3-phosphate
mutant I45Y, pH 7.4, 25°C
16
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
17.7
D-glyceraldehyde 3-phosphate
mutant I45F, pH 7.4, 25°C
20
D-glyceraldehyde 3-phosphate
mutant V167P/W168E, pH 7.5, 25°C
24
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
60
D-glyceraldehyde 3-phosphate
mutant P168A, 25°C, pH 7.6
67
D-glyceraldehyde 3-phosphate
pH 7.6, mutant enzyme Y74G
70.4
D-glyceraldehyde 3-phosphate
mutant C127S, pH 7.8, 30°C
72.8
D-glyceraldehyde 3-phosphate
mutant I45G, pH 7.4, 25°C
76.7
D-glyceraldehyde 3-phosphate
mutant V45A, pH 7.4, 25°C
78.3
D-glyceraldehyde 3-phosphate
mutant I45A, pH 7.4, 25°C
160
D-glyceraldehyde 3-phosphate
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
185
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96H
190
D-glyceraldehyde 3-phosphate
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
220
D-glyceraldehyde 3-phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
240
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G
261
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme K174G/T175G/A176G
330
D-glyceraldehyde 3-phosphate
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
483
D-glyceraldehyde 3-phosphate
-
mutant C14S/A73C, 25°C, pH 7.4
520
D-glyceraldehyde 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
600
D-glyceraldehyde 3-phosphate
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
620
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96S
740
D-glyceraldehyde 3-phosphate
mutant Y208A, pH 7.5, 25°C
750
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C
750
D-glyceraldehyde 3-phosphate
-
mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C
750
D-glyceraldehyde 3-phosphate
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
770
D-glyceraldehyde 3-phosphate
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
833
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
833
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
940
D-glyceraldehyde 3-phosphate
mutant Y208S, pH 7.5, 25°C
1100
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126S
1330
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
1330
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
1367
D-glyceraldehyde 3-phosphate
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
1373
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
1470
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
1570
D-glyceraldehyde 3-phosphate
mutant D213A, pH 7.5, 25°C
1600
D-glyceraldehyde 3-phosphate
mutant enzyme S227N
1650
D-glyceraldehyde 3-phosphate
mutant I45V, pH 7.4, 25°C
1666
D-glyceraldehyde 3-phosphate
presence of 2-carboxyethyl methanethiosulfonate
1830
D-glyceraldehyde 3-phosphate
mutant D213Q, pH 7.5, 25°C
1900
D-glyceraldehyde 3-phosphate
mutant I45L, pH 7.4, 25°C
2000
D-glyceraldehyde 3-phosphate
mutant K183S, pH 7.5, 25°C
2100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
2100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
2100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
2170
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C
2170
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C
2330
D-glyceraldehyde 3-phosphate
mutant K183A, pH 7.5, 25°C
2417
D-glyceraldehyde 3-phosphate
pH 7.6, mutant enzyme Y74C
2420
D-glyceraldehyde 3-phosphate
pH 7.6, mutant enzyme Y74C
2450
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, tetrameric enzyme form
2466
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96W
2500
D-glyceraldehyde 3-phosphate
mutant enzymeR191A
2600
D-glyceraldehyde 3-phosphate
mutant enzyme S227A
2600
D-glyceraldehyde 3-phosphate
-
mutant C14S/A69C, 25°C, pH 7.4
2670
D-glyceraldehyde 3-phosphate
-
mutant C15A, pH 7.4, 25°C
2690
D-glyceraldehyde 3-phosphate
mutant C218S, pH 7.8, 30°C
2800
D-glyceraldehyde 3-phosphate
mutant S211A, pH 7.5, 25°C
2967
D-glyceraldehyde 3-phosphate
-
mutant C14S/S79C, 25°C, pH 7.4
3100
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126A
3166
D-glyceraldehyde 3-phosphate
mutant W162F/W173F/W196F
3166
D-glyceraldehyde 3-phosphate
presence of methyl methanethiosulfonate
3200
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
3200
D-glyceraldehyde 3-phosphate
-
mutant C14S/S71C, 25°C, pH 7.4
3200
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
3333
D-glyceraldehyde 3-phosphate
mutant W162F
3372
D-glyceraldehyde 3-phosphate
in 100 mM triethanolamine (pH 7.4), at 25°C
3406
D-glyceraldehyde 3-phosphate
wild-type, pH 7.8, 30°C
3570
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH 7.6
3666
D-glyceraldehyde 3-phosphate
mutant W75F/W162F/W173F
3667
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14P
3670
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14P
3700
D-glyceraldehyde 3-phosphate
mutant Y208T, pH 7.5, 25°C
3830
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14T
3833
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14T
4000
D-glyceraldehyde 3-phosphate
-
-
4000
D-glyceraldehyde 3-phosphate
mutant enzyme R191S
4000
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14V
4160
D-glyceraldehyde 3-phosphate
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C
4166
D-glyceraldehyde 3-phosphate
mutant W196F
4170
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
4183
D-glyceraldehyde 3-phosphate
-
wild-type, 25°C, pH 7.4
4300
D-glyceraldehyde 3-phosphate
pH 7.0, 25°C
4300
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, wild-type enzyme
4300
D-glyceraldehyde 3-phosphate
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
4300
D-glyceraldehyde 3-phosphate
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25°C
4330
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, wild-type enzyme
4333
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, wild-type enzyme
4333
D-glyceraldehyde 3-phosphate
mutant W75F/W173F/W196F
4400
D-glyceraldehyde 3-phosphate
wild-type, pH 7.6, 25°C
4467
D-glyceraldehyde 3-phosphate
pH 7.6, wild-type enzyme
4467
D-glyceraldehyde 3-phosphate
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
4470
D-glyceraldehyde 3-phosphate
pH 7.6, wild-type enzyme
4500
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25°C
4500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
4600
D-glyceraldehyde 3-phosphate
-
mutant D225Q, pH 7.4, 25°C
4667
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme A238S
4670
D-glyceraldehyde 3-phosphate
-
mutant A238S
4670
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme A238S
4700
D-glyceraldehyde 3-phosphate
-
25°C, pH 7., wild-type enzyme
4833
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, dimeric enzyme form
5000
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14S
5000
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C
5000
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C
5133
D-glyceraldehyde 3-phosphate
-
mutant C14S, 25°C, pH 7.4
5167
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14A
5167
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
5167
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
5170
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25°C, mutant enzyme C14A
5170
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25°C
5300
D-glyceraldehyde 3-phosphate
mutant A178L, pH 7.6, 25°C
5500
D-glyceraldehyde 3-phosphate
mutant F12W
6000
D-glyceraldehyde 3-phosphate
wild-type enzyme
6000
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
6000
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
6166
D-glyceraldehyde 3-phosphate
mutant W173F
6170
D-glyceraldehyde 3-phosphate
-
-
6400
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
6900
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25°C
7000
D-glyceraldehyde 3-phosphate
-
wild type enzyme
7000
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
7020
D-glyceraldehyde 3-phosphate
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C
7166
D-glyceraldehyde 3-phosphate
mutant W75F/W162F/W196F
7300
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
7500
D-glyceraldehyde 3-phosphate
mutant S211G, pH 7.5, 25°C
7666
D-glyceraldehyde 3-phosphate
-
7666
D-glyceraldehyde 3-phosphate
wildtype
8000
D-glyceraldehyde 3-phosphate
mutant W75F
8670
D-glyceraldehyde 3-phosphate
-
-
8700
D-glyceraldehyde 3-phosphate
-
at pH 7.5 and 37°C
8900
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
9000
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
14670
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
15670
D-glyceraldehyde 3-phosphate
mutant D213A, pH 7.5, 25°C
16700
D-glyceraldehyde 3-phosphate
-
-
18330
D-glyceraldehyde 3-phosphate
mutant D213Q, pH 7.5, 25°C
20000
D-glyceraldehyde 3-phosphate
mutant K183S, pH 7.5, 25°C
23330
D-glyceraldehyde 3-phosphate
mutant K183A, pH 7.5, 25°C
42330
D-glyceraldehyde 3-phosphate
pH 7.6, wild-type enzyme
68330
D-glyceraldehyde 3-phosphate
-
22°C, pH 7.6
1430000
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
1548000
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
25000000
D-glyceraldehyde 3-phosphate
pH 8.0, 90°C
57500000
D-glyceraldehyde 3-phosphate
pH 8.0, 90°C
4.5
dihydroxyacetone 3-phosphate
mutant Y208F, pH 7.5, 25°C
135
dihydroxyacetone 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
210
dihydroxyacetone 3-phosphate
mutant Y208A, pH 7.5, 25°C
250
dihydroxyacetone 3-phosphate
mutant Y208S, pH 7.5, 25°C
327
dihydroxyacetone 3-phosphate
-
at pH 7.5 and 37°C
340
dihydroxyacetone 3-phosphate
wild-type, pH 7.5, 25°C
580
dihydroxyacetone 3-phosphate
mutant Y208T, pH 7.5, 25°C
810
dihydroxyacetone 3-phosphate
mutant S211G, pH 7.5, 25°C
860
dihydroxyacetone 3-phosphate
wild-type, pH 7.5, 25°C
0.06
dihydroxyacetone phosphate
monomeric mutant A178L, pH 7.6, 25°C
0.25
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
0.8
dihydroxyacetone phosphate
monomeric wild-type, pH 7.6, 25°C
4.7
dihydroxyacetone phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
6.5
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
8
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
19
dihydroxyacetone phosphate
mutant P168A, 25°C, pH 7.6
50
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G
54
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme K174G/T175G/A176G
60
dihydroxyacetone phosphate
-
25°C, pH 7.4, mutant enzyme C126S
267
dihydroxyacetone phosphate
-
25°C, pH 7.4, dimeric enzyme form
300
dihydroxyacetone phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
300
dihydroxyacetone phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
300
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
340
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
430
dihydroxyacetone phosphate
-
30°C, pH 7.6, wild-type enzyme
500
dihydroxyacetone phosphate
-
25°C, pH 7.4, wild-type enzyme
500
dihydroxyacetone phosphate
mutant A178L, pH 7.6, 25°C
645
dihydroxyacetone phosphate
wild-type, 25°C, pH 7.6
730
dihydroxyacetone phosphate
in 100 mM Tris pH 7.8, at 25°C
800
dihydroxyacetone phosphate
wild-type, pH 7.6, 25°C
63
glycerone phosphate
mutant enzyme R191A
180
glycerone phosphate
mutant enzyme D227A
200
glycerone phosphate
mutant enzyme D227N
240
glycerone phosphate
mutant enzyme R191S
367
glycerone phosphate
-
-
1000
glycerone phosphate
wild-type enzyme
1000
glycerone phosphate
-
recombinant enzyme
1080
glycerone phosphate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.012 - 120400000
D-glyceraldehyde 3-phosphate
0.26 - 750
dihydroxyacetone 3-phosphate
2 - 580
dihydroxyacetone phosphate
0.012
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
0.014
D-glyceraldehyde 3-phosphate
mutant 170-173del, pH 7.5, 25°C
0.47
D-glyceraldehyde 3-phosphate
mutant V167P/W168E, pH 7.5, 25°C
0.62
D-glyceraldehyde 3-phosphate
mutant lacking loop 3, pH 7.4, 25°C
0.9
D-glyceraldehyde 3-phosphate
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C
3.9
D-glyceraldehyde 3-phosphate
mutant lacking loop 3, pH 7.4, 25°C
5.4
D-glyceraldehyde 3-phosphate
mutant Y208F, pH 7.5, 25°C
12.2
D-glyceraldehyde 3-phosphate
mutant I45Y, pH 7.4, 25°C
28
D-glyceraldehyde 3-phosphate
mutant F96S, 25°C, pH not specified in the publication
28.5
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96S
29.6
D-glyceraldehyde 3-phosphate
mutant C127S/C218S, pH 7.8, 30°C
30
D-glyceraldehyde 3-phosphate
mutant F96Y, 25°C, pH not specified in the publication
33.3
D-glyceraldehyde 3-phosphate
mutant I45F, pH 7.4, 25°C
38
D-glyceraldehyde 3-phosphate
mutant F96S/S73A, 25°C, pH not specified in the publication
40.8
D-glyceraldehyde 3-phosphate
mutant I45G, pH 7.4, 25°C
59
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
70.5
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96H
84
D-glyceraldehyde 3-phosphate
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C
120
D-glyceraldehyde 3-phosphate
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
147
D-glyceraldehyde 3-phosphate
mutant C127S, pH 7.8, 30°C
149
D-glyceraldehyde 3-phosphate
mutant V45A, pH 7.4, 25°C
151
D-glyceraldehyde 3-phosphate
mutant T75N, pH 7.6, 23°C
160
D-glyceraldehyde 3-phosphate
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
198.3
D-glyceraldehyde 3-phosphate
mutant I45A, pH 7.4, 25°C
230
D-glyceraldehyde 3-phosphate
mutant S211A, pH 7.5, 25°C
240
D-glyceraldehyde 3-phosphate
mutant Y208S, pH 7.5, 25°C
260
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
260
D-glyceraldehyde 3-phosphate
mutant Y208A, pH 7.5, 25°C
280
D-glyceraldehyde 3-phosphate
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
296
D-glyceraldehyde 3-phosphate
mutant T75C, pH 7.6, 23°C
390
D-glyceraldehyde 3-phosphate
mutant F96S/L167V, 25°C, pH not specified in the publication
418
D-glyceraldehyde 3-phosphate
mutant T75V, pH 7.6, 23°C
440
D-glyceraldehyde 3-phosphate
mutant F96A, 25°C, pH not specified in the publication
475
D-glyceraldehyde 3-phosphate
mutant T75S, pH 7.6, 23°C
520
D-glyceraldehyde 3-phosphate
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
540
D-glyceraldehyde 3-phosphate
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
645
D-glyceraldehyde 3-phosphate
wild-type, pH 7.6, 23°C
730
D-glyceraldehyde 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
1100
D-glyceraldehyde 3-phosphate
mutant Y208T, pH 7.5, 25°C
1500
D-glyceraldehyde 3-phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
1601
D-glyceraldehyde 3-phosphate
mutant C218S, pH 7.8, 30°C
1933
D-glyceraldehyde 3-phosphate
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
2050
D-glyceraldehyde 3-phosphate
pH 7.6, mutant F96W
2580
D-glyceraldehyde 3-phosphate
wild-type, pH 7.8, 30°C
3250
D-glyceraldehyde 3-phosphate
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
4200
D-glyceraldehyde 3-phosphate
mutant S211G, pH 7.5, 25°C
5119
D-glyceraldehyde 3-phosphate
pH 7.0, 25°C
5467
D-glyceraldehyde 3-phosphate
mutant I45V, pH 7.4, 25°C
5800
D-glyceraldehyde 3-phosphate
-
at pH 7.5 and 37°C
5833
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
5833
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
5867
D-glyceraldehyde 3-phosphate
mutant I45L, pH 7.4, 25°C
6333
D-glyceraldehyde 3-phosphate
wild-type, pH 7.4, 25°C
6600
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
8400
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
8400
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
8400
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
8900
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
10500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
10850
D-glyceraldehyde 3-phosphate
pH 7.6, wild-type enzyme
11000
D-glyceraldehyde 3-phosphate
wild-type, pH 7.5, 25°C
11000
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
11500
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
11500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
12000
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
12000
D-glyceraldehyde 3-phosphate
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
12200
D-glyceraldehyde 3-phosphate
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25°C
12750
D-glyceraldehyde 3-phosphate
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
13600
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
857000
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
1269000
D-glyceraldehyde 3-phosphate
pH 8.0, 25°C
84880000
D-glyceraldehyde 3-phosphate
pH 8.0, 90°C
120400000
D-glyceraldehyde 3-phosphate
pH 8.0, 90°C
0.26
dihydroxyacetone 3-phosphate
mutant Y208F, pH 7.5, 25°C
10
dihydroxyacetone 3-phosphate
mutant S211A, pH 7.5, 25°C
10
dihydroxyacetone 3-phosphate
mutant Y208S, pH 7.5, 25°C
12
dihydroxyacetone 3-phosphate
mutant Y208A, pH 7.5, 25°C
34
dihydroxyacetone 3-phosphate
mutant Y208T/S211G, pH 7.5, 25°C
53
dihydroxyacetone 3-phosphate
mutant Y208T, pH 7.5, 25°C
250
dihydroxyacetone 3-phosphate
mutant S211G, pH 7.5, 25°C
510
dihydroxyacetone 3-phosphate
wild-type, pH 7.5, 25°C
580
dihydroxyacetone 3-phosphate
wild-type, pH 7.5, 25°C
750
dihydroxyacetone 3-phosphate
-
at pH 7.5 and 37°C
2
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
13
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
61
dihydroxyacetone phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
430
dihydroxyacetone phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
430
dihydroxyacetone phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
430
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
580
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.003
(1E,3E,6E,8E)-1,9-di(furan-2-yl)nona-1,3,6,8-tetraen-5-one
Trypanosoma cruzi
-
pH 7.4, 25°C
0.1
(1Z,2Z)-N,N'-dihydroxy-4-methylcyclohexa-3,5-diene-1,2-diimine
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
(2E)-2-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methylidene]hydrazinecarbothioamide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
(2E)-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarbothioamide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
(2E)-2-[2-[(3-oxido-2,1,3-benzoxadiazol-5-yl)methoxy]benzylidene]-N-(prop-2-en-1-yl)hydrazinecarbothioamide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
(2E)-N-(naphthalen-2-yl)-2-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]hydrazinecarboxamide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.03 - 0.1
(2E)-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarboxamide
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.0047
(2E,5E)-2,5-bis[(2E)-3-(thiophen-2-yl)prop-2-en-1-ylidene]cyclopentan-1-one
Trypanosoma cruzi
-
pH 7.4, 25°C
0.000086
(2E,6E)-2,6-bis[(2E)-3-(furan-2-yl)prop-2-en-1-ylidene]cyclohexan-1-one
Trypanosoma cruzi
-
pH 7.4, 25°C
0.0035
1,2,4-thiadiazole
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.013
1,2,6-thiadiazine
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.01
1,3,4-oxathiazole
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.03 - 0.1
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
2-phenyl-4H-chromen-4-one
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
2-[(1E)-2-nitroprop-1-en-1-yl]thiophene
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
3,5-diphenyl-1,2,4-thiadiazole
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
3-(4-methylphenyl)-5-[(4-methylphenyl)sulfonyl]-1,2,4-thiadiazole
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
3-nitrobiphenyl-4-amine
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
4-(4-nitrobenzylidene)-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.02
4-[(5-nitrofuran-2-yl)methylidene]-4H-1,2,6-thiadiazine-3,5-diamine 1,1-dioxide
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
4-[(5-nitrothiophen-2-yl)methylidene]-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
5-[(1E)-2-nitroprop-1-en-1-yl]-1,3-benzodioxole
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.03 - 0.1
6-[(E)-2-(5-nitrothiophen-2-yl)ethenyl]-2,1,3-benzoxadiazole 1-oxide
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.1
6-[(E)-2-[(4-fluorophenyl)sulfanyl]ethenyl]-2,1,3-benzoxadiazole 1-oxide
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.4
8-bromo-5,10-dioxidophenazin-2-yl chloroacetate
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.014
butylbrevifolin carboxylate
Trypanosoma cruzi
-
-
0.1
ethyl 3-(3,5-di-tert-butyl-4-hydroxyphenyl)-1,2,4-thiadiazole-5-carboxylate
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.03 - 0.1
ethyl 3-phenyl-1,2,4-thiadiazole-5-carboxylate
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.008
ethylbrevifolin carboxylate
Trypanosoma cruzi
-
-
0.0066
methylbrevifolin carboxylate
Trypanosoma cruzi
-
-
0.1
N-[(2-oxido-4-phenyl-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
Trypanosoma cruzi
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.026
phenazine 5,9-dioxide
Trypanosoma cruzi
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36°C
0.154 - 0.57
phosphoenolpyruvate
0.154
phosphoenolpyruvate
Homo sapiens
-
mutant I170T, pH not specified in the publication, temperature not specified in the publication
0.193
phosphoenolpyruvate
Homo sapiens
-
mutant I170V, pH not specified in the publication, temperature not specified in the publication
0.57
phosphoenolpyruvate
Homo sapiens
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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?
-
x * 27000, SDS-PAGE
?
-
x * 27600, SDS-PAGE
-
?
x * 28000, SDS-PAGE, recombinant protein with His-tag
?
-
x * 28000, SDS-PAGE, recombinant protein with His-tag
-
?
-
x * 27832, electrospray mass spectrometry
?
-
x * 25000, SDS-PAGE
-
?
-
x * 30000, about, SDS-PAGE
?
-
x * 30000, about, SDS-PAGE
-
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 26500, SDS-PAGE, both wild-type and mutant M80T
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
loop-loop interactions in the dimer play a role in coordinating motions and enzymatic function in triosephosphate isomerase, NMR and circular dichroism spectroscopy structure analysis of wild-type and mutant enzymes, overview
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 27000, SDS-PAGE
dimer
-
primary structure of subunit
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 27000, SDS-PAGE
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
2 * 28108, mass spectrometry
dimer
-
2 * 28108, mass spectrometry
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
two types of subunits possess similar but distinguishable amino acid composition, 3 electrophorectic forms: AA, AB, BB
dimer
-
2 * 26500-27300, SDS-PAGE, subunit composition of the three forms A, B, and C is alpha2, alpha,beta, and beta2
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 27000, SDS-PAGE of denatured cytosolic enzyme
dimer
-
2 * 28000, SDS-PAGE
dimer
structure comparisons, overview
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 28213, mass spectrometry, 2 * 30000, SDS-PAGE
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 28213, mass spectrometry, 2 * 30000, SDS-PAGE
-
dimer
-
X-ray crystallography, only the TIM dimer is fully active
-
dimer
-
each subunit contains an active site
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
x-ray crystallography
dimer
2 * 27000, gel filtration and SDS-PAGE, the active site of triosephosphate isomerase lies very close to the subunit interface, a network of key interactions spans the interacting subunits
dimer
2 * 55663, electrospray mass spectrometry
dimer
TIM is functional only as a homodimer, the interface Cys13 plays a major role in the stability of the dimer, Cys13 forms favorable interactions with loop 3 and Lys12. Structurally conserved Tyr74 may be essential for the stability, it is necessary to preserve the collective motions in the dimer that contribute to the catalytic efficiency of the TIM dimer. Tyr74 is a ready-made recognition motif for TIM homodimerization
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
2 * 27829, and monomer, mass spectrometry
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
the low stability of the monomers is neither the only, nor the main, cause for the dimeric nature of the enzyme
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 28000, SDS-PAGE
dimer
-
2 * 26500, cytosolic enzyme, SDS-PAGE
dimer
-
2 * 27000, chloroplastic enzyme, SDS-PAGE
dimer
-
2 * 27000, SDS-PAGE of denatured cytosolic enzyme
dimer
gel filtration and SDS-PAGE, crystal structure, overview
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
2 * 27000, calculated from sequence
dimer
-
wild-type enzyme consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
-
2 * 27244, calculation from nucleotide sequence
dimer
X-ray crystallography, only the TIM dimer is fully active
hexamer
6 * 23000, SDS-PAGE
hexamer
-
6 * 23000, SDS-PAGE
-
homodimer
2 * 28249, calculated from amino acid sequence
homodimer
2 * 28266, MALDI-TOF mass spectrometry
homodimer
-
2 * 26732, calculated from amino acid sequence
homodimer
-
2 * 27600, estimated from SDS-PAGE
homodimer
-
2 * 27600, estimated from SDS-PAGE
-
homodimer
2 * 27000, SDS-PAGE
homodimer
2 * 27188, calculated from amino acid sequence
homotetramer
-
4 * 27800, SDS-PAGE
homotetramer
-
4 * 27800, SDS-PAGE
-
homotetramer
4 * 24000, SDS-PAGE
homotetramer
-
4 * 24000, SDS-PAGE
-
monomer
1 * 27 831, electrospray mass spectrometry
monomer
1 * 27829, and dimer, mass spectrometry
monomer
-
1 * 26879, equilibrium sedimentation
tetramer
-
4 * 27000, SDS-PAGE
tetramer
X-ray diffraction data
tetramer
4 * 25000, SDS-PAGE
tetramer
-
4 * 24000, crystallographic data
tetramer
4 * 25000, SDS-PAGE
tetramer
assembled as a dimer of dimers
additional information
-
tetramer results from covalent attachment of two dimers that conserve similar association constants between their constituent monomers
additional information
-
in a yeast two-hybrid system, enzyme interacts with integrin alphaIIb cytoplasmic domain and binds weakly to its alphaV tail
additional information
secondary and tertiary structure analysis of the enzyme in monomeric and dimeric states by mass spectrometry, circular dichromism, and fluorescence spectroscopy, and by crystal structure analysis, at pH 1.8-6.8 and 20-80°C, detailed overview. Detection of four forms of the dimeric, glycolytic enzyme TIM, which are assigned to the dimer, a folded monomer, a partially unfolded state and a largely unfolded monomeric species. Water molecules tightly bound to all the four forms
additional information
-
secondary and tertiary structure analysis of the enzyme in monomeric and dimeric states by mass spectrometry, circular dichromism, and fluorescence spectroscopy, and by crystal structure analysis, at pH 1.8-6.8 and 20-80°C, detailed overview. Detection of four forms of the dimeric, glycolytic enzyme TIM, which are assigned to the dimer, a folded monomer, a partially unfolded state and a largely unfolded monomeric species. Water molecules tightly bound to all the four forms
additional information
simulation of the dynamics of monomeric TIM subunit A, molecular dynamics simulations, disulfide cross-linking at the interface is required for stability, the absence of a disulfide bond between Cys13 and Cys74 produces a dramatic shift in the conformation of Lys12, overview
additional information
-
simulation of the dynamics of monomeric TIM subunit A, molecular dynamics simulations, disulfide cross-linking at the interface is required for stability, the absence of a disulfide bond between Cys13 and Cys74 produces a dramatic shift in the conformation of Lys12, overview
additional information
occurence of dimer and monomer in solution. The decreasing order of dimer stability is wild-type > T75S > Q64E = Q64N
additional information
-
occurence of dimer and monomer in solution. The decreasing order of dimer stability is wild-type > T75S > Q64E = Q64N
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
additional information
structure analysis and loop interactions of TIM, overview
additional information
-
structure analysis and loop interactions of TIM, overview
additional information
in solution the enzyme exhibits an equilibrium between inactive dimers and active tetramers
additional information
-
in solution the enzyme exhibits an equilibrium between inactive dimers and active tetramers
additional information
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three-dimensional structure and peptide mapping, the residues K155, D158, W159, A160 and K16 form a continuous patch at the surface of the enzyme
additional information
-
reversible guanidinium hydrochloride induced equilibrium unfolding involves stable dimeric and monomeric intermediates
additional information
structure determination and analysis of the monomeric enzyme, overview
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sitting drop vapor diffusion method, using either 65% (v/v) 2-methyl-2,4-pentanediol 0.1 M HEPES, pH 7.5, or 6% (w/v) PEG 6000 0.1 M HEPES, pH 7.0, or 17.5% (w/v) PEG 3350, 0.1 M Bis-Tris, pH 5.5, or 15% (w/v) PEG 3350 0.1 M Bis-Tris, pH 5.0
using 100 mM Bis-Tris propane pH 7.5, 200 mM sodium sulfate, 20% (w/v) PEG 3350
crystals are grown at 18°C from hanging drops by mixing 0.005 ml of the enzyme, 5 mg/ml, with 0.005 ml of the reservoir solution, 28% w/v PEG 1500 and 0.001 ml of 30% v/v 1,6-hexanediol
-
crystal structure of the recombinant enzyme complexed with phosphoglycolohydroxamate, at 1.8 A resolution
-
simulation of both dimeric and monomeric (isolated from dimer) forms in explicit water at 27°C and 1 bar. Significant cross-correlations between residue fluctuations are observed in the dimer, which result from the global counter-rotations of the two identical subunits in the essential modes of the dimer. The first essential mode contributing to 34% of overall motion of the dimer is strongly coupled to the loop 6's closure over the active site. The monomeric structure maintains relatively localized motions of the loops in the essential modes
structures of mutants 170-173del and V167P/W168E
hanging drop vapor diffusion method
-
triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution
-
determination of intrinsic fluorescence of wild-type and mutants lacking Trp residues, interpretation based on crystal structure. Fluorescence of all Trp residues is quenched by aromatic-aromatic interactions due to the proximity and orientation of the indole groups of Trp196 and Tro162. Quenching is also due to energy transfer to the charged resiudes that surround Trp75, Trp173, and Trp196
determination by molecular replacement, at 2.3 A resolution and in the closed state. Phosphate acts as a competitive inhibitor and occupies the binding pocket. Binding pocket has a very stable conformation even without a substrate
monomer, to 2.3 A resolution
high resolution structure of crystal form 2 employing the gel-tube method in microgravity
-
mutant E104D, at 1.85 A resolution. Mutant structure is similar to wild-type, mutant residue E104A is part of a conserved cluster of 10 residues, 5 from each subunit. This cluster forms a cavity that possesses an elaborate conserved network of buried water molecules that bridge the two subunits. In the E104D mutant, a disruption of contacts of the amino acid side chains in the conserved cluster leads to a perturbation of the water network in which the water-protein and water-water interactions that join the two monomers are significantly weakened and diminished
triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution
-
crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
-
mutant enzyme E65Q, hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
purified enzyme mutant E65Q in complex with reaction-intermediate analogue phosphoglycolohydroxamate, hanging drop method, TIM-PGH crystals are grown at room temperature, 0.004 ml of protein solution with 11 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl, 10 mM PGH, 1 mM DTT, 1 mM EDTA, and 1 mM NaN3, are mixed with 0.004 ml of well solution containing 0.1M acetate, pH 5.0, 24% PEG6000, 1 mM DTT, 1 mM EDTA, and 1 mM NaN3, X-ray diffraction structure determination and analysis at 0.82 A resolution
unliganded enzyme. Complete absence of electron density for the loop 6 residues. Disorder of this loop due to a missing slat bridge between residues at the N-and C-terminal ends of the loop
crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex, at 2.7 A resolution
-
hanging drop vapor diffusion method. Crystal structure of the enzyme-sulfate complex and the enzyme-2-phosphoglycolate complex at a 2.7 A resolution
-
hanging drop vapor diffusion method, using 16% (w/v) PEG 3350 and 250 mM ammonium citrate
hanging drop vapor diffusion method, apo-enzyme structure, refined to 1.5 A resolution, in which the active site loop is either in the open or in the closed conformation in different subunits of the enzyme. The observation of both open and closed lid conformations in triosephosphate isomerase crystals might by related to a persistent conformational heterogeneity of the protein in solution
structure of TPI with bound phosphoenolpyruvate at 1.6 A resolution. Phosphoenolpyruvate is bound to the catalytic pocket of TPI and occludes substrate
two crystal forms, A and B, belonging to space group P212121 are obtained by hanging-drop method. Crystal form A has unit-cell parameters a = 65.14, b = 72.45, c = 93.24 A and diffracts to 2.25 A at -188°C, whereas form B has unit-cell parameters A = 73.02, b = 79.8 and c = 172.85
-
crystal structure analysis
crystal structure analysis, overview
crystal structure of PfTIMat 2.2 A resolution or 2.8 A resolution, crystal structure of the enzyme in complex with phosphoglycolate at 1.9 A resolution, crystal structure of the enzyme in complex with glycerol phosphate at 2.4 A resolution, crystal structure of the enzyme in complex with 2-phosphoglycerate at 1.1 A resolution or 2.4 A resolution
E97Q and E97D mutant enzymes, hanging drop vapor diffusion method
enzyme in complex with 3-phosphoglycerate or glycerol 3-phosphate, hanging drop vapor diffusion method
mutant enzyme C126S in complex with PGA, hanging drop vapor diffusion method, using 20% (w/v) poly(ethylene glycol), 1 M HEPES buffer (pH 7.5), and 10 mM lithium sulfate, at 23°C. Unliganded mutant enzymes C126S and C126A, hanging drop vapor diffusion method, using 24% (w/v) poly(ethylene glycol), 1 M HEPES buffer (pH 7.0), and 10 mM lithium sulfate
structures of wild-type and mutants at residues T75 and Q64
wild-type and mutant enzymes in complex with inhibitor 3-phosphoglycerate, 0.003 ml of 10 mg/ml protein in 100 mM triethanolamine-HCl, pH 7.6, are mixed with an equal volume of reservoir solution, the crystallization cocktail contains 0.1 M sodium acetate pH 4.0-5.5 and PEG 1450 varying from 8% to 24% in the reservoir, X-ray diffraction structure determination and analysis at 1.4-2.25 A resolutions
hanging drop vapor diffusion method, diffraction quality can only be obtained in the presence of inhibitors, monoclinic crystal form is obtained by cocrystallization with 20 mM 2-carboxyethylphosphonic acid with sodium acetate, pH 4.0, and 7% PEG 4000 as the precipitant buffer. An orthorhombic crystal form is obtained by cocrystallization with 20 mM 2-phosphoglycolic acid with 0.1 M sodium acetate, pH 4.2, and 5% PEG 4000 as the precipitant buffer. Hexagonal crystal forms are obtained under the same conditions with 2-phosphoglycolic acid, but their diffraction shows high disorder
-
hanging drop vapor diffusion method, using 0.1 M HEPES-Na, pH 7.5, and 1.4 M trisodium citrate dihydrate
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
enzyme alone and in complex with various phosphate containing ligands like glycerol 3-phosphate, glycerol 2-phosphate, 3-phosphoglyceric acid, and 2-phosphoglyceric acid, hanging drop vapor diffusion method
purified recombinant enzyme by hanging drop vapour diffusion method, from 1.6 M trisodium citrate dihydrate, pH 6.5, X-ray diffraction structure determination and analysis at1.9 A resolution, modeling
-
purified recombinant C-terminally His6-tagged enzyme, sitting drop vapour diffusion method, room temperature, 0.003 ml of 18 mg/ml protein in 10 mM MES buffer, pH 6.5, and 15 mM NaCl, is mixed with 0.003 ml of reservoir solution containing 18% PEG MME 2000 as precipitant, X-ray diffraction structure determination and analysis at 2.0 A resolution
structures of apo- and glycerol-3-phosphate-bound TPI, to 1.94 and 2.17 A resolution, respectively. The protein adopts the canonical TIM-barrel fold with eight alpha-helices and parallel eight beta-strands
structure of both a hexagonal and an orthorhombic crystal form to resolutions of 2.5 A and 2.3 A. In both crystal forms the enzyme exists as a tetramer of the (betaalpha)8-barrel. Hexagonal crystal form (crystallisation conditions 0.1 M HepesKOH (pH 7.5), 0.8 M sodium potassium phosphate) diffracts to 2.5 A and belongs to spacegroup P6(5)22/P6(1)22 with cell dimensions a = b = 186.9 A, c = 287.8 A, alpha = beta = 90°, gamma = 120°, suggesting two tetramers in the asymmetric unit. Orthorhombic crystals with cell dimensions a = 154.1 A, b = 91.0 A, c = 141.2 A, alpha = beta = gamma = 90° are obtained in 0.1 M sodium acetate (pH 4.6), 0.2 M ammonium sulfate, with PEG4000 at any concentration between 20% and 30% (w/v). Crystals grew within 48 hours at 20°C
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method, crystal structure represents the most thermostable triosephosphate isomerase presently known in its 3D-structure
use of real time in situ atomic force microscopy to monitor the molecular processes that govern the crystallization of triosephosphate isomerase. Triosephosphate isomerase tetramers are the dominating growth units. The incorporation of growth units occurs through surface diffusion. Normal growth is dominated by the two-dimensional nucleation of triangular islands
monomeric enzyme variant with an engineered binding groove, m18bTIM, and the V233A mutant of this variant in complex with citrate, 2-phosphoglycolate, and glycerol 3-phosphate, to 1.89, 1.6, 2.3 and 2.0 A resolution, respectively
mutant A178L, unliganded and in complex with 2-phosphoglycolate, to 2.2 A and 1.89 A, respectively. Monomeric mutant mlA178L, unliganded and in complex with 2-phosphoglycolate, to 2.3 A and 1.18 A, respectively. Mutation A178L favors the closed conformation of the C-terminal hinge region
mutant enzyme R191S, hanging drop vapor diffusion method, crystal structure of the R191S mutant complexed with 2-phosphoglycolate is determined at 1.65 A resolution
mutant P168A, with and without 2-phosphoglycolate. Phosphate moiety of 2-phosphoglycolate is bound similarly as in wild-type, but interactions of the carboxylic acid moiety with the side chain of catalytic Glu167 differ
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
hanging drop vapor diffusion method, a crystal of the dimeric enzyme is soaked and diffracted in hexane and its structure solved at 2 A resolution. Its overall structure and the dimer interface are not altered by hexane
hanging drop vapour diffusion method, crystals of the enzyme in complex with one molecule of 3-(2-benzothiazolylthio)-1-propanesulfonic acid diffract to a resolution of 2 A. Unit cell dimensions: a = 42.87, b = 75.57, c = 146.45
molecular docking studies with inhibitors
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purified recombinant monomeric enzyme by sitting drop method, 0.001 ml of protein solutioncontaining 25 mg/ml protein in 20 mM Tris-HCl , pH 7.4, and 1.0 mM EDTA is mixed with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 7.5, 10% PEG 6000, and 5% MPD, X-ray diffraction structure determination and analysis
comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms
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genetically engineered enzyme variant, at 2.6 A resolution
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resolution of 2.1 A in a new crystal form grown at pH 8.8 from PEG6000
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C127S
loss of more than 97% of specific activity
C127S/C218S
loss of more than 97% of specific activity
C218S
loss of about 21% of specific activity. In presence of glutathione disulfide, mutant behaves similarly to the wild-type, but retains more activity than the wild-type after 240 min of incubation
M80T
-
analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis
170-173del
loop deletion mutant, 800000fold decrease in kcat/Km value
K174G/T175G/A176G
-
16.5fold decrease in turnover number for D-glyceraldehyde 3-phosphate, 7.9fold increase in Km-value for D-glyceraldehyde 3-phosphate, 8fold decrease in turnover number for dihydroxyacetone phosphate, 2.6fold increase in Ki-value for arsenate, 10.4fold increase in Ki-value for 2-phosphoglycolate
L7RM
-
the mutant exhibits a 200fold decrease in kcat/Km for isomerization of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The mutant exhibits a 25fold decrease in kcat/Km for deprotonation of glycolaldehyde catalyzed by free enzyme. The mutation has little effect on the observed and intrinsic phosphodianion binding energy and only a modest effect on phosphite dianion activation of the enzyme
V167G/W168G
-
17.9fold decrease in turnover number for D-glyceraldehyde 3-phosphate, 2.6fold increase in Km-value for D-glyceraldehyde 3-phosphate, 8.6fold decrease in turnover number for dihydroxyacetone phosphate, 2.7fold increase in Ki-value for arsenate, 8.1fold increase in Ki-value for 2-phosphoglycolate
V167G/W168G/K174G/T175G/A176G
-
2529fold decrease in turnover number for D-glyceraldehyde 3-phosphate, 8.5fold increase in Km-value for D-glyceraldehyde 3-phosphate, 1720fold decrease in turnover number for dihydroxyacetone phosphate, 2.8fold increase in Ki-value for arsenate, 12.4fold increase in Ki-value for 2-phosphoglycolate
V167P/W168E
loop replacement mutant, 23000fold decrease in kcat/Km value. Mutations result in large displacement of the side chain of E168 from that for W168 in wild-type. Binding of glycerol 3-phosphate results in chemical shift changes for nuclei at the active site that are smaller than those of wild-type
Y208T/G210A/S211G
-
site-directed mutagenesis
H12N
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 64°C compared to 68°C for the wild-type enzyme
H12N/K13G
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 37°C compared to 68°C for the wild-type enzyme
H13G
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 51°C compared to 68°C for the wild-type enzyme
F12W
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W162F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W162F/W173F/W196F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W173F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W196F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W75F
mutant constructed for fluorescence quenching studies, catalytic properties similar to wild-type
W75F/W162F/W173F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W75F/W162F/W196F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W75F/W173F/W196F
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
I170T
-
13% residual activity
K13R
-
mutant is catalytically inactive and largely unstable
E65Q
the variant of Leishmania mexicana TIM has a much enhanced stability but its catalytic properties are the same as wild-type leishmanial TIM
C126A
the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme
C126M
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme
C126S
the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme
C126T
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme
C126V
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme
C13D
the mutant displays significant reduction in catalytic activity when compared with wild type enzyme (about 7.4fold decrease in kcat). The C13D mutant dissociates at concentrations above 1.25 mM
C13E
the mutant displays significant reduction in catalytic activity when compared with wild type enzyme (about 3.3fold decrease in kcat). The C13E mutant retains dimeric at concentrations above 1.25 mM
E165A
the mutant shows an approximately 9000fold drop in activity
E97D
the mutant shows a 100fold reduction in kca
E97Q
the mutant shows a 4000fold reduction in kca
F96A
considerable loss in acitivity
F96H
site-directed mutagenesis, the mutant exhibits highly reduced catalytic efficiency and decreased substrate-binding affinity, as well as reduced sensitivity to inhibitor 3-phosphoglycerate, compared to the wild-type enzyme
F96S/L167V
considerable loss in acitivity
F96S/S73A
considerable loss in acitivity
F96W
site-directed mutagenesis, the mutant exhibits reduced catalytic efficiency and decreased substrate-binding affinity, as well as reduced sensitivity to inhibitor 3-phosphoglycerate, compared to the wild-type enzyme. The wild-type enzyme shows a loop-open state for 3-phosphoglycerate binding at the active site, while the mutant F96W shows both open and closed states
F96Y
considerable loss in acitivity
T75C
activity similar to wild-type, dimer integrity is unimpaired. Decrease in stability between 35°C and 45°C
T75N
4fold drop in activity compared to wild-type. Decrease in stability between 35°C and 45°C
T75V
activity similar to wild-type, dimer integrity is unimpaired. Decrease in stability between 35°C and 45°C
W11F/W168F/Y74W
site-directed mutagenesis, template is the available crystal structure of the enzyme from Giardia lamblia, which contains a Trp residue at position 47. The mutant dissociates at low protein concentrations, and exhibits considerably reduced stability in the presence of denaturants, urea and guanidinium chloride, and it shows approximately 20fold reduction in kcat at low protein concetrations compared to the wild-type enzyme, but the mutant mutant shows an enhancement of activity of 21.9fold at higher concentration range
Y74G
site-directed mutagenesis, the mutation Tyr74Gly significantly reduces the stability of the dimer, mutation-induced alteration in the backbone conformation of Lys12, structure comparison to the wild-type enzyme
R111T/R112A/E114K/E115G
-
site-directed mutagenesis, destroying of four ion pair interactions by replacing four of the charged residues in helix 4 with structurally analogous residues from the psychrophile Methanococcoides burtonii TIM to create a mutant, mPfuTIM, that is less kinetically stable than wild-type PfuTIM
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
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
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
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
Y208T/S211G
tenfold decrease in kcat/Km
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
-
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
-
H12N/K13G
-
mutant enzyme shows increases thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 96°C compared to 94°C of the wild-type enzyme
I45F
dimer-monomer equilibrium
I45G
142fold decrease in catalytic activity
I45L
dimeric, CD spectrum is identical to wild-type
I45V
dimeric, CD spectrum is identical to wild-type
I45Y
monomeric, 479fold decrease in catalytic activity
V45A
29fold less active than wild-type. Mutant dissociates into stable monomers and assembles as catalytic competent dimer upon binding of the transition state substrate analog phosphoglycolohydroxamate
A178L
decrease in catalytic efficiency. Crystallization data reveal a more disordered loop-6 in the structure of unliganded A178L. Liganded structures show minimal differences to wild-type
C14A
-
the KM-value for D-glyceraldehyde 3-phosphate is 1.2fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is 90% of the value for the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 1.2fold higher than the value for the wild-type enzyme. The turnover-number for glycerone phosphate is comparable to the value for the wild-type enzyme
C14F
-
the Ki-value for 3-phosphoglycolate is nearly 3times higher than the Ki-value for the wild-type enzyme. The ratio of elimination to isomerization reactions is higher than in the wild-type enzyme. The KM-value for D-glyceraldehyde 3-phosphate is 10.2fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is 2.7fold higher than the value for the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 2280fold lower than the value for the wild-type enzyme. The turnover-number for glycerone phosphate is 3000fold lower than the value for the wild-type enzyme
C14L
-
Cys14Leu mutant has the tendency to aggregate, reduced stability and altered kinetics
C14P
-
the KM-value for D-glyceraldehyde 3-phosphate is 94% of the value for the wild-type enzyme. The KM-value for glycerone phosphate is 58% of the value for the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 85% of the value for the wild-type enzyme. The turnover-number for glycerone phosphate is 81% of the value for the wild-type enzyme
C14S/A69C
-
similar in kinetic parameters to wild-type TbTIM and the single mutant C14S. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14S/A73C
-
greatly reduced kcat value. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14S/S71C
-
similar in kinetic parameters to wild-type TbTIM and the single mutant C14S. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14S/S79C
-
similar in kinetic parameters to wild-type TbTIM and the single mutant C14S. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14T
-
the KM-value for D-glyceraldehyde 3-phosphate is 1.2fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is 79% of the value of the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 92% of the value for the wild-type enzyme. The turnover-number for glycerone phosphate is 92% of the value of the wild-type enzyme
D227A
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42°C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 2.2fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 5fold lower than the value for the wild-type enzyme
D227N
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42°C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 3.75fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 3.5fold lower than the value for the wild-type enzyme
E168D
-
catalytically inert. Dimer formation with Trypanosoma cruzi dimer interface mutant C15Acauses a drop in activity by 50%
H47N
-
mutant His47Asn, dimer is considerably less stable than wild-type trypanosomal enzyme
P168A
mutation beside catalytic residue Glu167. Mutant turnover number is 50fold reduced, Km value is 2fold reduced
R191A
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42°C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 10.4fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 10.6fold lower than the value for the wild-type enzyme
R191S
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42°C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 2fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 6.7fold lower than the value for the wild-type enzyme
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
F28L/A100L/A115Q
mutant constructed to mimick the methylmethane sulfonate inactivation pattern of the Trypanosoma cruzi enzyme. Protein is similarly susceptibel to methylmethane sulfonate as the Trypanosoma cruzi enzyme
L232A
-
the mutation in a 6fold decrease in kcat/Km for the reversible isomerization of D-glyceraldehyde 3-phosphate to give dihydroxyacetone phosphate
P168A
-
the mutation results in 50fold decrease in kcat/Km for deprotonation of glycolaldehyde catalyzed by free enzyme
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
S43P
mutation increases the free energy of the transition state by 17.7 kJ/mol
C15A
-
dimer formation of mutant protein with intact Trypanosoma brucei monomer, maximal inhibition of catalysis by mutation is 60%. Dimer formation with catalytically inert Trypanosoma brucei mutant E168D causes a drop in activity by 50%
E26D/T27L/L28F/A30S/L100A/Q115A
mutant construcuted to produce a TIM with the inactivation susceptibility pattern of Trypanosoma brucei brucei enzyme, shows a similar resistance pattern to the inactivation with methylmethane thiosulfonate as wild-type Trypanosoma brucei brucei TIM
E26D/T27L/L28F/A30S/T32S/L100A/Q115A
mutant construcuted to produce a TIM with the inactivation susceptibility pattern of Trypanosoma brucei brucei enzyme, shows a similar resistance pattern to the inactivation with methylmethane thiosulfonate as wild-type Trypanosoma brucei brucei TIM
E26D/T27L/L28F/L100A/Q115A
mutant construcuted to produce a TIM with the inactivation susceptibility pattern of Trypanosoma brucei brucei enzyme, shows a similar resistance pattern to the inactivation with methylmethane thiosulfonate as wild-type Trypanosoma brucei brucei TIM
L28F/L100A/Q115A
mutant construcuted to produce a TIM with the inactivation susceptibility pattern of Trypanosoma brucei brucei enzyme. Protein is more resistant to the inactivation with methylmethane thiosulfonate as wild-type
D213A
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
D213A
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
D213Q
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
D213Q
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
K183A
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
K183A
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
K183S
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
K183S
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
E104D
mutation involved in human triosephosphate isomerase defiecency autosomal disease. Mutant exhibits normal catalytic activity but shows impairments in the formation of active dimers and low thermostability. E104A is part of a conserved cluster of 10 residues, 5 from each subunit. This cluster forms a cavity that possesses an elaborate conserved network of buried water molecules that bridge the two subunits. In the E104D mutant, a disruption of contacts of the amino acid side chains in the conserved cluster leads to a perturbation of the water network in which the water-protein and water-water interactions that join the two monomers are significantly weakened and diminished
E104D
in patients homozygous for this mutation, only 2-20% of TIM catalytic activity is left
I170V
the mutation is asociated with a mild form of TIM deficiency
I170V
-
5.9% residual activity
A238S
-
mutant enzyme A238S has a higher thermal stability than the wild-type enzyme. The turnover number of the mutant enzyme is somewhat lower than that observed for the wild-type enzyme, the Km-value for D-glyceraldehyde 2-phosphate is somewhat higher
A238S
-
catalytic efficiency of the mutant enzyme is somewhat reduced, and its stability is considerably increased. The half-life at 25°C is 27 min compared to 10 min for the wild-type enzyme
F96S
site-directed mutagenesis, the mutant exhibits highly reduced catalytic efficiency and decreased substrate-binding affinity, as well as reduced sensitivity to inhibitor 3-phosphoglycerate, compared to the wild-type enzyme
F96S
300fold drop in kcat/Km
Q64E
mutation at key dimer interface residue, decreases dimer stability
Q64E
mutation weakens the dimeric structure
Q64N
mutation at key dimer interface residue, decreases dimer stability
Q64N
mutation weakens the dimeric structure
T75S
activity similar to wild-type, dimer integrity is unimpaired. Decrease in stability between 35°C and 45°C
T75S
mutation at key dimer interface residue, decreases dimer stability
Y74C
inhibitory effect of KFGNGSYTGEVS and KYGNGSCTGEVS is more pronounced compared to the wild-type enzym. Mutant enzyme has reduced stability due to an interface cavity
Y74C
-
urea unfolding profiles of Y74Cox in urea solution obtained by fluorescence and circular dichroism approximate a two-state transition and do not show the presence of stable intermediates over a wide range of denaturant concentrations. In wild-type enzyme the unfolding results in gradual change in spectroscopic properties. The unfolding transition midpoit is 3.5 M for Y74Cox and 5.5 M for the wild-type enzyme
I45A
29fold decrease in activity. Residue I45 controls the dimer-monomer equilibrium, mutant displays a dimer-monomer equilibrium and is stable
I45A
39fold less active than wild-type. Mutant dissociates into stable monomers and assembles as catalytic competent dimer upon binding of the transition state substrate analog phosphoglycolohydroxamate
C14S
-
the KM-value for D-glyceraldehyde 3-phosphate is 1.4fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is identical to the value of the wild-type value. The turnover number for D-glyceraldehyde 3-phosphate is 1.15fold higher than the value for the wild-type enzyme. The turnover-number for glycerone phosphate is nearly identical to the value of the wild-type enzyme
C14S
-
wild-type-like enzyme that is resistant to the action of sulfhydryl reagents methylmethane thiosulfonate and 5,5-dithiobis(2-nitrobenzoate)
additional information
construction of a T-DNA insertion mutant that shows a fivefold reduction in transcript, reduced TPI activity, and a severely stunted and chlorotic seedling that accumulates dihydroxyacetone phosphate, glycerol, and glycerol-3-phosphate. Methylglyoxal, a by-product of dihydroxyacetone phosphate, also accumulated in the pdtpi mutant. Lipid profiling reveals lower monogalactosyl but higher digalactosyl lipids in the mutant compared to the wild-type, phenotype, overview. Exogenous glycolytic intermediates do not rescue the pdtpi phenotype. Metabolic pathways affected by a mutation in pdTPI during postgerminative seedling transition from heterotrophic to photoautotrophic development, overview
additional information
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construction of a T-DNA insertion mutant that shows a fivefold reduction in transcript, reduced TPI activity, and a severely stunted and chlorotic seedling that accumulates dihydroxyacetone phosphate, glycerol, and glycerol-3-phosphate. Methylglyoxal, a by-product of dihydroxyacetone phosphate, also accumulated in the pdtpi mutant. Lipid profiling reveals lower monogalactosyl but higher digalactosyl lipids in the mutant compared to the wild-type, phenotype, overview. Exogenous glycolytic intermediates do not rescue the pdtpi phenotype. Metabolic pathways affected by a mutation in pdTPI during postgerminative seedling transition from heterotrophic to photoautotrophic development, overview
additional information
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mutation wasted away is a recessive, hypomorphic mutation that causes progressive motor impairment, vacuolar neuropthology, and severely reduced lifespan. Mutation affects the gene for triosephosphate isomerase. There is no genetic evidence that the mutation leads to misfolded or aberrant protein. Mutation may lead to an accumulation of methylglyoxal and the consequent enhanced production of advanced glycation end products
additional information
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overexpression of isoform Tpi2 in a Tpi1-deficient mutant restores the growth deficiency on minimal medium containing glucose or glycerol
additional information
overexpression of isoform Tpi2 in a Tpi1-deficient mutant restores the growth deficiency on minimal medium containing glucose or glycerol
additional information
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Tpi1-deficient mutant grows weakly on minimal medium containing glucose or glycerol, but grows normally on gluconate. Residual enzymic activity on glucose or glycerol is due to presence of enzyme isoform Tpi2
additional information
Tpi1-deficient mutant grows weakly on minimal medium containing glucose or glycerol, but grows normally on gluconate. Residual enzymic activity on glucose or glycerol is due to presence of enzyme isoform Tpi2
additional information
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modulation of gene expression around wild-type level by replacing the native promoter with libraries of synthetic promoters. Enzyme is present in high excess in wild-type cells. 10% residual activity still support more than 70% of the wild-type glycolytic flux. At at residual triosephosphate isomerase activity of 3%, dihydroxyacetone phosphate level increases four times and coincides with an increase in formate production
additional information
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some TPIs are found on the paired helical filaments in Tau transgenic mice
additional information
decrease in ligand affinity in F96 mutants can be a consequence of differences in the water network connecting residue 96 to Ser73 in the vicinity of the active site
additional information
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decrease in ligand affinity in F96 mutants can be a consequence of differences in the water network connecting residue 96 to Ser73 in the vicinity of the active site
additional information
expression of enzyme confers arsenic tolerance to Escherichia coli XL1 Blue and DF502
additional information
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expression of enzyme confers arsenic tolerance to Escherichia coli XL1 Blue and DF502
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
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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
a mutant lacking loop 3 is 1500fold less active than wild-type and dissociates into stable monomers. Upon binding of the transition state substrate analog phosphoglycolohydroxamate, mutant remains monomeric
additional information
a mutant lacking loop 3 is 1500fold less active than wild-type and dissociates into stable monomers. Upon binding of the transition state substrate analog phosphoglycolohydroxamate, mutant remains monomeric
additional information
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a mutant lacking loop 3 is 1500fold less active than wild-type and dissociates into stable monomers. Upon binding of the transition state substrate analog phosphoglycolohydroxamate, mutant remains monomeric
additional information
a mutant lacking loop 3 is 9400fold less active than wild-type and dissociates into stable monomers. Upon binding of the transition state substrate analog phosphoglycolohydroxamate, mutant remains monomeric
additional information
a mutant lacking loop 3 is 9400fold less active than wild-type and dissociates into stable monomers. Upon binding of the transition state substrate analog phosphoglycolohydroxamate, mutant remains monomeric
additional information
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a mutant lacking loop 3 is 9400fold less active than wild-type and dissociates into stable monomers. Upon binding of the transition state substrate analog phosphoglycolohydroxamate, mutant remains monomeric
additional information
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wild-type enzyme consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit. By replacing 15 residues of the major interface loop by another 8-residue fragment, a variant is constructed that is a stable and monomeric protein with TIM activity, monoTIM. The turnover numer of the monomeric form is 100fold lower
additional information
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hybrids of Trypanosoma cruzi enzyme carrying residues of the dimer interface from Trypanomsoma brucei and vice versa, and hybrids with one monomer in the enzyme dimer from Trypanosoma cruzi, and the second monomer from Trypanosoma brucei. Solvent exposure of the interfacial C15 depends predominantly on the characteristics of the adjoining monomer. Half of the activity of each monomer depends on the integrity of each of the two C15-loop3 portions of the interface
additional information
introduction of mutation V233A into a monomeric enzyme variant with an engineered binding groove, m18bTIM. Mutation V233A restores the structural properties of loop-7, the binding site of a conserved water molecule between loop-7 and loop-8 and the binding site of the phosphate moiety of wild-type in the m18bTIM background. The active site of the V233A mutant can bind transition state analogs and suicide inhibitors competently, the catalytic efficiency of the V233A mutant is too low to be detected
additional information
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a reporter protein fused to a Saccharomyces cerevisiae peptide containing the sequence corresponding to the 22-residue fragment, including residues K155, D158, W159, A160 and K161, of the Trypanosoma brucei TPI enzyme, is not targeted to glycosomes
additional information
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the monomeric form of TIM does not catalyze any reactions of D-glyceraldehyde 3-phosphate at the enzyme active site, either in the absence or in the presence of phosphite dianion
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
additional information
construction of mutants for interconversion of the behavior of the enzymes from Trypanosoma brucei brucei and Trypanosoma cruzi. To make Trypanosoma cruzi TIM reactivate with a Trypanosoma brucei brucei TIM-like behaviour you need to mutate the following amino acids: 18, 19, 20, 22, 23 and 26, and R2: 43, 46, 48, 49, 53, 56 and 57. To make a Trypanosoma brucei brucei TIM reactivate with a Trypanosoma cruzi TIM-like behaviour you need to mutate amino acids 18, 23, 26, 32, 33 and 34, and 43, 46, 48, 49, 53, 56 and 57
additional information
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hybrids of Trypanosoma cruzi enzyme carrying residues of the dimer interface from Trypanomsoma brucei and vice versa, and hybrids with one monomer in the enzyme dimer from Trypanosoma cruzi, and the second monomer from Trypanosoma brucei. Solvent exposure of the interfacial C15 depends predominantly on the characteristics of the adjoining monomer. Half of the activity of each monomer depends on the integrity of each of the two C15-loop3 portions of the interface
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
additional information
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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
additional information
construction of mutants for interconversion of the behavior of the enzymes from Trypanosoma brucei brucei and Trypanosoma cruzi. To make Trypanosoma cruzi TIM reactivate with a Trypanosoma brucei brucei TIM-like behaviour you need to mutate the following amino acids: 18, 19, 20, 22, 23 and 26, and R2: 43, 46, 48, 49, 53, 56 and 57. To make a Trypanosoma brucei brucei TIM reactivate with a Trypanosoma cruzi TIM-like behaviour you need to mutate amino acids 18, 23, 26, 32, 33 and 34, and 43, 46, 48, 49, 53, 56 and 57
additional information
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construction of mutants for interconversion of the behavior of the enzymes from Trypanosoma brucei brucei and Trypanosoma cruzi. To make Trypanosoma cruzi TIM reactivate with a Trypanosoma brucei brucei TIM-like behaviour you need to mutate the following amino acids: 18, 19, 20, 22, 23 and 26, and R2: 43, 46, 48, 49, 53, 56 and 57. To make a Trypanosoma brucei brucei TIM reactivate with a Trypanosoma cruzi TIM-like behaviour you need to mutate amino acids 18, 23, 26, 32, 33 and 34, and 43, 46, 48, 49, 53, 56 and 57
additional information
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construction of a monomeric enzyme form with loop-1 one residue shorter than monoTIM, which is constructed by replacing 15 residues of the major interface loop by another 8-residue fragment. The catalytic activity and stability of the new seven-residue Loop-1 enzyme variant is similar with that of monoTIM
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