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
-
assemblage
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aldolase
-
duodenalis
-
dihydroxyacetone
-
enolase
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phosphoglycerate
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zoonotic
-
barrel
-
fecal
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trypanosoma
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multilocus
-
fructose
-
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
-
province
-
cysts
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malate
-
stool
-
lamblia
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methylglyoxal
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phosphofructokinase
-
cruzi
-
schistosoma
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enediolate
-
2-phosphoglycolate
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parvum
-
hemolytic
-
intestinalis
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fructose-1,6-bisphosphate
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deamidation
-
alpha-enolase
-
1,6-bisphosphate
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glucosephosphate
-
tim-barrel
-
hungarian
-
hominis
-
phosphite
-
dianion
-
phosphoglucose
-
glycosomes
-
enzymopathy
-
fructose-bisphosphate
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ige-binding
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subgenotype
-
diagnostics
-
synthesis
-
analysis
-
biofuel production
-
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
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Reaction
Reaction on EC 5.3.1.1 - triose-phosphate isomerase
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D-Glyceraldehyde 3-phosphate = glycerone phosphate
in situ magnetic resonance probes of the enzyme-bound substrates to test the question of whether the equilibrium concentrations are perturbed by the enzyme. In the exergonic conversion of glycerinaldehyde 3-phosphate to dihydroxyacetone phosphate the high discrimination against solvent isotope uptake is consistent with chemistry protected by a water-tight active-site loop, therefore introducing asymmetry into the reversible reaction
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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
upon binding of ligand, the side chain of Glu167 flips from the inactive swung-out to the active swung-in conformation. A concerted movement of loop 6 and loop 7 from unliganded-open to liganded-closed is facilitated by the interactions of the phosphate moiety with loop 7. Rotation of the Gly211-Gly212 peptide plane of 90° is involved in this concerted movement
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
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D-Glyceraldehyde 3-phosphate = glycerone phosphate
reaction mechanism via enediolate intermediate through proton abstraction by the catalytic base Glu167, overview