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
5.3.1.1 triose-phosphate isomeraseAdvanced search results
results (
results (Subunits
Subunits on EC 5.3.1.1 - triose-phosphate isomerase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
hexamer
homodimer
homotetramer
monomer
tetramer
additional information
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
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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
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two types of subunits possess similar but distinguishable amino acid composition, 3 electrophorectic forms: AA, AB, BB
dimer
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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
X-ray crystallography, only the TIM dimer is fully active
dimer
-
X-ray crystallography, only the TIM dimer is fully active
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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
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
-
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
-
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
additional information
-
tetramer results from covalent attachment of two dimers that conserve similar association constants between their constituent monomers
additional information
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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
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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
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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
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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
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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
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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
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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
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reversible guanidinium hydrochloride induced equilibrium unfolding involves stable dimeric and monomeric intermediates
additional information
structure determination and analysis of the monomeric enzyme, overview
