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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Trypanosoma cruzi and UniProt Accession P52270
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EC Tree
5.3.1.1 triose-phosphate isomeraseSpecify your search results
Word Map
- 5.3.1.1
- giardia
-
assemblage
- aldolase
- duodenalis
- dihydroxyacetone
- enolase
- phosphoglycerate
-
zoonotic
-
barrel
-
fecal
- trypanosoma
-
multilocus
- fructose
- giardiasis
- dhap
- cryptosporidium
- brucei
-
protozoan
- isomerases
- gapdh
-
province
- cysts
- malate
-
stool
- lamblia
- methylglyoxal
-
phosphofructokinase
- cruzi
- schistosoma
-
enediolate
- 2-phosphoglycolate
- parvum
-
hemolytic
- intestinalis
- fructose-1,6-bisphosphate
-
deamidation
- alpha-enolase
- 1,6-bisphosphate
-
glucosephosphate
-
tim-barrel
-
hungarian
- hominis
- phosphite
-
dianion
-
phosphoglucose
- glycosomes
-
enzymopathy
-
fructose-bisphosphate
-
ige-binding
-
subgenotype
- diagnostics
- synthesis
- analysis
- biofuel production
- medicine
The taxonomic range for the selected organisms is: Trypanosoma cruzi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
triosephosphate isomerase, triose phosphate isomerase, triose-phosphate isomerase, tctim, pftim, gltim, monotim, pfutim, cp 25, cytoplasmic tpi, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CP 25
-
-
-
-
D-glyceraldehyde-3-phosphate ketol-isomerase
-
-
-
-
Isomerase, triose phosphate
-
-
-
-
Lactacin B inducer protein
-
-
-
-
monoTIM
-
-
-
-
PfTIM
-
-
-
-
Phosphotriose isomerase
-
-
-
-
TIM
Triose phosphate isomerase
-
-
-
-
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
TIM
-
-
-
-
Triosephosphate isomerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
CAS REGISTRY NUMBER
COMMENTARY
9023-78-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
(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
(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
2,2'-methylenebis(1,3-benzothiazole)
-
40% inactivation at 0.05 mM, irreversible
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor
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
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
ethyl 3-(3,5-di-tert-butyl-4-hydroxyphenyl)-1,2,4-thiadiazole-5-carboxylate
-
-
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
methylbrevifolin carboxylate
-
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
-
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
additional information
-
brevifolin carboxylate derivatives isolated from Geranium bellum selectively inactivate the enzyme partially, no inhibition by methyl tri-O-methylbrevifolin carboxylate
-
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
0.28
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C
0.31
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C
0.43
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 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
0.69
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5167
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
750
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, 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
2170
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C
4500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
5000
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11500
D-glyceraldehyde 3-phosphate
wild-type, 25°C, pH not specified in the publication
10500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.1
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
0.1
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 60% of maximal activity, pH 9.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TPIS_TRYCR
251
0
27329
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
structure determination and analysis of the monomeric enzyme, overview
additional information
-
reversible guanidinium hydrochloride induced equilibrium unfolding involves stable dimeric and monomeric intermediates
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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%
additional information
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
-
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
-
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant monomeric enzyme from Escherichia coli strain BL21 (DE3)
ammonium sulfate precipitation, Toyopearl column chromatography and SP-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the monomeric enzyme in Escherichia coli strain BL21 (DE3)
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
unfolding/refolding reactions of monomeric enzyme evaluated using the two-state model
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
systematic mutagenesis method to find critical residues for certain physico-chemical properties of a protein. The method is a shorter alternative to random mutagenesis, saturation mutagenesis or directed evolution to find multiple amino acids critical for certain properties of proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ostoa-Saloma, P.; Garza-Ramos, G.; Ramirez, J.; Becker, I.; Berzunza, M.; Landa, A.; Gomez-Puyou, A.; Tuena de Gomez-Puyou, M.; Perez-Montfort, R.
Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi
Eur. J. Biochem.
244
700-705
1997
Leishmania mexicana, Trypanosoma brucei, Trypanosoma cruzi
Gao, X.G.; Maldonado, E.; Perez-Montfort, R.; Garza-Ramos, G.; de Gomez-Puyou, M.T.; Gomez-Puyou, A.; Rodriguez-Romero, A.
Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane
Proc. Natl. Acad. Sci. USA
96
10062-10067
1999
Trypanosoma cruzi (P52270), Trypanosoma cruzi
Chanez-Cardenas, M.E.; Perez-Hernandez, G.; Sanchez-Rebollar, B.G.; Costas, M.; Vazquez-Contreras, E.
Reversible equilibrium unfolding of triosephosphate isomerase from Trypanosoma cruzi in guanidinium hydrochloride involves stable dimeric and monomeric intermediates
Biochemistry
44
10883-10892
2005
Trypanosoma cruzi
Tellez-Valencia, A.; Olivares-Illana, V.; Hernandez-Santoyo, A.; Perez-Montfort, R.; Costas, M.; Rodriguez-Romero, A.; Lopez-Calahorra, F.; Tuena De Gomez-Puyou, M.; Gomez-Puyou, A.
Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface
J. Mol. Biol.
341
1355-1365
2004
Trypanosoma cruzi (P52270), Trypanosoma cruzi
Olivares-Illana, V.; Perez-Montfort, R.; Lopez-Calahorra, F.; Costas, M.; Rodriguez-Romero, A.; Tuena de Gomez-Puyou, M.; Gomez Puyou, A.
Structural differences in triosephosphate isomerase from different species and discovery of a multitrypanosomatid inhibitor
Biochemistry
45
2556-2560
2006
Leishmania mexicana, Trypanosoma brucei, Trypanosoma cruzi
Zomosa-Signoret, V.; Aguirre-Lopez, B.; Hernandez-Alcantara, G.; Perez-Montfort, R.; Tuena de Gomez-Puyou, M.; Gomez-Puyou, A.
Crosstalk between the subunits of the homodimeric enzyme triosephosphate isomerase
Proteins Struct. Funct. Bioinform.
67
75-83
2007
Trypanosoma brucei, Trypanosoma cruzi
Zarate-Perez, F.; Chanez-Cardenas, M.E.; Arreola, R.; Torres-Larios, A.; Vazquez-Contreras, E.
Different catalytic properties of two highly homologous triosephosphate isomerase monomers
Biochem. Biophys. Res. Commun.
382
626-630
2009
Trypanosoma cruzi (P52270)
Gayosso-De-Lucio, J.; Torres-Valencia, M.; Rojo-Dominguez, A.; Najera-Pena, H.; Aguirre-Lopez, B.; Salas-Pacheco, J.; Avitia-Dominguez, C.; Tellez-Valencia, A.
Selective inactivation of triosephosphate isomerase from Trypanosoma cruzi by brevifolin carboxylate derivatives isolated from Geranium bellum Rose
Bioorg. Med. Chem. Lett.
19
5936-5939
2009
Trypanosoma cruzi
Wierenga, R.K.; Kapetaniou, E.G.; Venkatesan, R.
Triosephosphate isomerase: a highly evolved biocatalyst
Cell. Mol. Life Sci.
67
3961-3982
2010
Entamoeba histolytica (O02611), Oryctolagus cuniculus (P00939), Gallus gallus (P00940), Saccharomyces cerevisiae (P00942), Geobacillus stearothermophilus (P00943), Trypanosoma brucei brucei (P04789), Escherichia coli (P0A858), Giardia intestinalis (P36186), Thermotoga maritima (P36204), Leishmania mexicana (P48499), Moritella marina (P50921), Trypanosoma cruzi (P52270), Helicobacter pylori (P56076), Homo sapiens (P60174), Pyrococcus woesei (P62003), Mycobacterium tuberculosis (P9WG43), Plasmodium falciparum (Q07412), Caenorhabditis elegans (Q10657), Methanocaldococcus jannaschii (Q58923), Bartonella henselae (Q8L1Z5), Tenebrio molitor (Q8MPF2), Thermoproteus tenax (Q8NKN9), Mycobacterium tuberculosis H37Rv (P9WG43)
Alvarez, G.; Aguirre-Lopez, B.; Varela, J.; Cabrera, M.; Merlino, A.; Lopez, G.V.; Lavaggi, M.L.; Porcal, W.; Di Maio, R.; Gonzalez, M.; Cerecetto, H.; Cabrera, N.; Perez-Montfort, R.; de Gomez-Puyou, M.T.; Gomez-Puyou, A.
Massive screening yields novel and selective Trypanosoma cruzi triosephosphate isomerase dimer-interface-irreversible inhibitors with anti-trypanosomal activity
Eur. J. Med. Chem.
45
5767-5772
2010
Homo sapiens, Trypanosoma cruzi, Trypanosoma cruzi T2
Garcia-Torres, I.; Cabrera, N.; Torres-Larios, A.; Rodriguez-Bolanos, M.; Diaz-Mazariegos, S.; Gomez-Puyou, A.; Perez-Montfort, R.
Identification of amino acids that account for long-range interactions in two triosephosphate isomerases from pathogenic trypanosomes
PLoS ONE
6
e18791
2011
Trypanosoma brucei, Trypanosoma cruzi
Aguilera, E.; Varela, J.; Birriel, E.; Serna, E.; Torres, S.; Yaluff, G.; de Bilbao, N.; Aguirre-Lopez, B.; Cabrera, N.; Diaz Mazariegos, S.; de Gomez-Puyou, M.; Gomez-Puyou, A.; Perez-Montfort, R.; Minini, L.; Merlino, A.; Cerecetto, H.; Gonzalez, M.; Alvarez, G.
Potent and selective inhibitors of Trypanosoma cruzi triosephosphate isomerase with concomitant inhibition of cruzipain Inhibition of parasite growth through multitarget activity
ChemMedChem
17
1328-1338
2016
Trypanosoma cruzi, Trypanosoma cruzi Tulahuen 2
Rodriguez-Bolanos, M.; Cabrera, N.; Perez-Montfort, R.
Identification of the critical residues responsible for differential reactivation of the triosephosphate isomerases of two trypanosomes
Open biology
6
160161
2016
Trypanosoma brucei brucei (P04789), Trypanosoma cruzi (P52270), Trypanosoma cruzi
Diaz-Mazariegos, S.; Cabrera, N.; Perez-Montfort, R.
Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes
PLoS ONE
13
e0189525
2018
Trypanosoma brucei brucei (P04789), Trypanosoma cruzi (P52270)
Guzman-Luna, V.; Quezada, A.G.; Diaz-Salazar, A.J.; Cabrera, N.; Perez-Montfort, R.; Costas, M.
The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes
Proteins
85
571-579
2017
Trypanosoma brucei brucei (P04789), Trypanosoma cruzi (P52270), Trypanosoma cruzi
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