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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Entamoeba histolytica and UniProt Accession O02611

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Entamoeba histolytica
UNIPROT: O02611 not found.
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The taxonomic range for the selected organisms is: Entamoeba histolytica
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triosephosphate isomerase
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-78-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bromohydroxyacetone phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
methylmethane thiosulfonate
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0.6 mM, 2 h, complete loss of activity, dissociates the dimeric enzyme inducing formation of a compact monomeric state
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
optimum is near pH 8.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPIS_ENTHI
261
0
27935
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
X-ray crystallography, only the TIM dimer is fully active
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
50 min, no loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at a concentration of 2 ng/ml or 0.4 ng/ml stable for 24 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as wild-type enzyme and fusion protein with an N-terminal tail of six histidine residues
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
study on thermal dissociation and unfolding of enzyme and a monomeric variant obtained by chemical derivatization. During wild-type unfolding, sequential transitions corresponding to dimer dissociation into a compact monomeric intermediate followed by unfolding and further aggregation of the intermediate occurr. In the case of the monomeric variant, a single transition, analogous to the second transition of wild-type, is observed. Dimer dissociation is not restricted to localized interface reorganization. Dissociation represents 55% of the total enthalpy change. Subunit assembly is probably best represented by a fly-casting mechanism
study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Saccharomyces cerevisiae. Monomer unfolding is reversible for both enzymes, the dissociation step is reversible in yeast and irreversible in Entamoeba histolytica. Monomer unfolding induced by high pressure in presence of guanidinium hydrochloride is reversible. In the absence of denaturants, pressure would induce monomer unfolding prior to dimer dissociation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Landa, A.; Rojo-Dominguez, A.; Jimenez, L.; Fernandez-Velasco, D.A.
Sequencing, expression and properties of triosephosphate isomerase from Entamoeba histolytica
Eur. J. Biochem.
247
348-355
1997
Entamoeba histolytica, Trypanosoma brucei
Manually annotated by BRENDA team
Rodriguez-Romero, A.; Hernandez-Santoyo, A.; del Pozo Yauner, L.; Kornhauser, A.; Fernandez-Velasco, D.A.
Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica
J. Mol. Biol.
322
669-675
2002
Entamoeba histolytica
Manually annotated by BRENDA team
Vazquez-Perez, A.R.; Fernandez-Velasco, D.A.
Pressure and denaturants in the unfolding of triosephosphate isomerase: the monomeric intermediates of the enzymes from Saccharomyces cerevisiae and Entamoeba histolytica
Biochemistry
46
8624-8633
2007
Saccharomyces cerevisiae, Entamoeba histolytica
Manually annotated by BRENDA team
Tellez, L.A.; Blancas-Mejia, L.M.; Carrillo-Nava, E.; Mendoza-Hernandez, G.; Cisneros, D.A.; Fernandez-Velasco, D.A.
Thermal unfolding of triosephosphate isomerase from Entamoeba histolytica: dimer dissociation leads to extensive unfolding
Biochemistry
47
11665-11673
2008
Entamoeba histolytica (O02611), Entamoeba histolytica
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team