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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00939
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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: Oryctolagus cuniculus
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
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-
-
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D-glyceraldehyde-3-phosphate ketol-isomerase
-
-
-
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Isomerase, triose phosphate
-
-
-
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Lactacin B inducer protein
-
-
-
-
monoTIM
-
-
-
-
PfTIM
-
-
-
-
Phosphotriose isomerase
-
-
-
-
TIM
Triose phosphate isomerase
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
-
-
-
-
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
TIM
-
-
-
-
Triose phosphate isomerase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Glyceraldehyde 3-phosphate = glycerone phosphate
intrinsic binding energy of the substrate phosphodianion group is utilized to drive closing of the mobile loop and a protein conformational change that leads to formation of an active site environment that is optimally organized for stabilization of the transition state for proton transfer from R-carbonyl carbon
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D-Glyceraldehyde 3-phosphate = glycerone 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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
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CAS REGISTRY NUMBER
COMMENTARY
9023-78-3
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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
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
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
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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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
glycolytic regulation requires direct catalytic inhibition of TPI by the pyruvate kinase substrate phosphoenolpyruvate
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_RABIT
249
0
26757
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56000
-
sucrose density gradient centrifugation, equilibrium ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
dissociation/unfolding is a highly cooperative transition in which the ternary and the secondary structures of the protein are concomitantly lost. Isolation of two conformational isomers of the enzyme that exhibit significantly different stabilities and kinetics of unfolding
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.0, 2.5 mM ammonium sulfate, 1 mM EDTA, stable for at least 2 years
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
two conformational isomers of the enzyme that exhibit significantly different stabilities and kinetics of unfolding. Complete unfolding of the two isolated conformers at a 1.5 M guanidine-HCl followed by refolding by removal of the denaturant completely abolishes the differences in their unfolding kinetics
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
enzymatic synthesis of D-xylulose 5-phosphate using triosephosphate isomerase and transketolase. Comparison of use of glyceraldehyde 3-phosphate or dihydroxyacetone phosphate as starting substrate by process modeling via the use of windows of operation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krietsch, W.K.G.
Triosephosphate isomerase from rabbit liver
Methods Enzymol.
41B
438-442
1975
Oryctolagus cuniculus
-
Hartman, F.C.; Norton, I.L.
Triosephosphate isomerase from rabbit muscle
Methods Enzymol.
41B
447-453
1975
Oryctolagus cuniculus
Esnouf, M.P.; Harris, R.P.; McVittie, J.D.
Triosephosphate isomerase from chicken and rabbit muscle
Methods Enzymol.
89
579-583
1982
Gallus gallus, Oryctolagus cuniculus
Kessler, H.; Matter, H.; Geyer, A.; Diehl, H.J.; Kck, M.; Kurz, G.; Opperdoes, F.R.; Callens, M.; Wierenga, R.K.
Selektive Inhibierung der trypanosomalen Triosephosphat-Isomerase durch ein Thiopeptid
Angew. Chem.
104
343-345
1992
Canis lupus familiaris, Oryctolagus cuniculus, Escherichia coli, Trypanosoma sp.
-
Kuntz, D.A.; Osowski, R.; Schudok, M.; Wierenga, R.K.; Muller, K.; Kessler, H.; Opperdoes, F.R.
Inhibition of triosephosphate isomerase from Trypanosoma brucei wirth cyclic hexapeptides
Eur. J. Biochem.
207
441-447
1992
Canis lupus familiaris, Oryctolagus cuniculus, Escherichia coli, Trypanosoma brucei
Carza-Ramos, G.; Perez-Montfort, R.; Rojo-Dominguez, A.; de Gomez-Puyou, M.T.; Gomez-Puyou, A.
Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase
Eur. J. Biochem.
241
114-120
1996
Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Schizosaccharomyces pombe
Aparicio, R.; Ferreira, S.T.; Leite, N.R.; Polikarpov, I.
Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM)
Acta Crystallogr. Sect. D
56
1492-1494
2000
Oryctolagus cuniculus
-
Moreau, V.H.; Rietveld, A.W.; Ferreira, S.T.
Persistent conformational heterogeneity of triosephosphate isomerase: separation and characterization of conformational isomers in solution
Biochemistry
42
14831-14837
2003
Oryctolagus cuniculus
Aparicio, R.; Ferreira, S.T.; Polikarpov, I.
Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity
J. Mol. Biol.
334
1023-1041
2003
Oryctolagus cuniculus (P00939), Oryctolagus cuniculus
O'Donoghue, A.C.; Amyes, T.L.; Richard, J.P.
Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of (R)-glyceraldehyde 3-phosphate in D2O
Biochemistry
44
2610-2621
2005
Oryctolagus cuniculus
Fonvielle, M.; Mariano, S.; Therisod, M.
New inhibitors of rabbit muscle triose-phosphate isomerase
Bioorg. Med. Chem. Lett.
15
2906-2909
2005
Oryctolagus cuniculus
Amyes, T.L.; Richard, J.P.
Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion
Biochemistry
46
5841-5854
2007
Oryctolagus cuniculus
Shaeri, J.; Wright, I.; Rathbone, E.B.; Wohlgemuth, R.; Woodley, J.M.
Characterization of enzymatic D-xylulose 5-phosphate synthesis
Biotechnol. Bioeng.
101
761-767
2008
Oryctolagus cuniculus
ODonoghue, A.C.; Amyes, T.L.; Richard, J.P.
Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O
Org. Biomol. Chem.
6
391-396
2008
Oryctolagus cuniculus
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)
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