5.3.1.1: triose-phosphate isomerase
This is an abbreviated version!
For detailed information about triose-phosphate isomerase, go to the full flat file.
Word Map on EC 5.3.1.1
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5.3.1.1
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giardia
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assemblage
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aldolase
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duodenalis
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dihydroxyacetone
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enolase
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phosphoglycerate
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zoonotic
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barrel
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fecal
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trypanosoma
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multilocus
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fructose
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giardiasis
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dhap
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cryptosporidium
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brucei
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protozoan
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isomerases
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gapdh
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province
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cysts
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malate
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stool
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lamblia
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methylglyoxal
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phosphofructokinase
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cruzi
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schistosoma
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enediolate
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2-phosphoglycolate
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parvum
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hemolytic
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intestinalis
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fructose-1,6-bisphosphate
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deamidation
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alpha-enolase
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1,6-bisphosphate
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glucosephosphate
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tim-barrel
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hungarian
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hominis
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phosphite
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dianion
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phosphoglucose
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glycosomes
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enzymopathy
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fructose-bisphosphate
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ige-binding
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subgenotype
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diagnostics
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synthesis
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analysis
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biofuel production
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medicine
- 5.3.1.1
- giardia
-
assemblage
- aldolase
- duodenalis
- dihydroxyacetone
- enolase
- phosphoglycerate
-
zoonotic
-
barrel
-
fecal
- trypanosoma
-
multilocus
- fructose
- giardiasis
- dhap
- cryptosporidium
- brucei
-
protozoan
- isomerases
- gapdh
-
province
- cysts
- malate
-
stool
- lamblia
- methylglyoxal
-
phosphofructokinase
- cruzi
- schistosoma
-
enediolate
- 2-phosphoglycolate
- parvum
-
hemolytic
- intestinalis
- fructose-1,6-bisphosphate
-
deamidation
- alpha-enolase
- 1,6-bisphosphate
-
glucosephosphate
-
tim-barrel
-
hungarian
- hominis
- phosphite
-
dianion
-
phosphoglucose
- glycosomes
-
enzymopathy
-
fructose-bisphosphate
-
ige-binding
-
subgenotype
- diagnostics
- synthesis
- analysis
- biofuel production
- medicine
Reaction
Synonyms
CP 25, CTIMC, cTPI, cytoplasmic TPI, cytoplasmic triosephosphate isomerase, cytoTPI, D-glyceraldehyde-3-phosphate ketol-isomerase, GlTIM, Isomerase, triose phosphate, Lactacin B inducer protein, monoTIM, PfTIM, PfuTIM, Phosphotriose isomerase, plastidic TPI, plastidic triosephosphate isomerase, pTPI, SSO2592, TcTIM, TIM, TIM1, TIM2, TonTIM, TpI, TPI1, TpiA, Triose phosphate isomerase, Triose phosphate mutase, Triose phosphoisomerase, Triosephosphate isomerase, Triosephosphate mutase, vTIM
ECTree
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Inhibitors
Inhibitors on EC 5.3.1.1 - triose-phosphate isomerase
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(1E,3E,6E,8E)-1,9-di(furan-2-yl)nona-1,3,6,8-tetraen-5-one
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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
(2E)-2-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methylidene]hydrazinecarbothioamide
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(2E)-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarbothioamide
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irreversible inhibitor
(2E)-2-[2-[(3-oxido-2,1,3-benzoxadiazol-5-yl)methoxy]benzylidene]-N-(prop-2-en-1-yl)hydrazinecarbothioamide
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irreversible inhibitor
(2E)-N-(naphthalen-2-yl)-2-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]hydrazinecarboxamide
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irreversible inhibitor
(2E)-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarboxamide
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irreversible inhibitor
(2E,5E)-2,5-bis[(2E)-3-(thiophen-2-yl)prop-2-en-1-ylidene]cyclopentan-1-one
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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
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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
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
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irreversible inhibitor
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
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
4-(4-nitrobenzylidene)-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
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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
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irreversible inhibitor
4-[(5-nitrothiophen-2-yl)methylidene]-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
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irreversible inhibitor
6-[(E)-2-(5-nitrothiophen-2-yl)ethenyl]-2,1,3-benzoxadiazole 1-oxide
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irreversible inhibitor
6-[(E)-2-[(4-fluorophenyl)sulfanyl]ethenyl]-2,1,3-benzoxadiazole 1-oxide
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irreversible inhibitor
cyclo[Trp-Tyr(OSO3Na)-D-Phe-Thr(OSO3Na)-Lys(benzyloxycarbonyl)-]
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noncompetitive, reversible
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
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GSSG
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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
methylbrevifolin carboxylate
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molecular docking simulations and enzyme binding structure, and inhibition kinetics, overview
N-[(2-oxido-4-phenyl-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
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72% inhibition at 0.4 mM
N-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
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41% inhibition at 0.4 mM
2,2'-methylenebis(1,3-benzothiazole)
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40% inactivation at 0.05 mM, irreversible
2-Phosphoglycolate
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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
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
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
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irreversible inactivation. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
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irreversible inactivation. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
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91% inactivation at 0.05 mM, irreversible. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
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
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
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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
about 50% inhibition at about 0.05 mM
methyl methanethiosulfonate
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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
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the sensitivity of enzyme from Trypanosoma cruzi is about 40times higher than that of Trypanosoma brucei and 200times higher than that of Leishmania mexicana
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0.6 mM, 2 h, complete loss of activity, dissociates the dimeric enzyme inducing formation of a compact monomeric state
methylmethane thiosulfonate
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induces 75% enzyme inactivation within 15 min at 0.25 mM concentration
methylmethane thiosulfonate
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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
inactivation by sulfhydroxylation
methylmethane thiosulfonate
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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
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
the reaction-intermediate analogue binds to the active site with two hydrogen-bonding interactions between PGH and the Glu167 side-chain oxygen atoms
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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
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additional information
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TPI phosphorylation by cyclin A/Cdk2 kinase leads to reduced TPI activity, prevented by treatment with olomoucine, a specific inhibitor of Cdk2
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additional information
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not inhibited by 1,2,6-thiadiazine, phenazine 5,9-dioxide, and 1,3,4-oxathiazole
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additional information
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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
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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
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additional information
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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
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additional information
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stronger inhibition by alpha-(1,3)-mannooligosaccharides than with triose, binding constants, overview
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additional information
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brevifolin carboxylate derivatives isolated from Geranium bellum selectively inactivate the enzyme partially, no inhibition by methyl tri-O-methylbrevifolin carboxylate
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