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
-
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
- 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
Advanced search results
Temperature Stability
Temperature Stability on EC 5.3.1.1 - triose-phosphate isomerase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
25
25 - 60
-
the recombinant enzyme is stable at 25°C for 30 min. The recombinant enzyme retains 92.7%, 40% and 13% activity when preincubated at 37°C, 42°C and 60°C for 30 min, respectively
25 - 95
-
no or limited loss of activity at pH 7.0 and pH 10.0, respectively, 50% loss of activity at pH 3.0. Cooling from 95°C induces cold denaturation in partially denatured TIM
42
50
60
63
if denaturation is carried out at temperatures above 64.0°C, a partially folded species is formed in a time short enough to avoid the occurence of deleterious aggregation reactions
64
90
additional information
25
-
half-life of wild-type enzyme: 10 min, half-life of mutant enzyme A238S: 27 min
42
half-life of wild-type enzyme: 180 min, half-life of mutant enzyme D227N: 128 min, half-life of mutant enzyme D227A: 122 min, half-life of mutant enzyme R191S: 87 min, half-life of mutant enzyme R191A: 124 min
-
Lys13 plays a crucial role in the functional adaptation of the thermophilic enzyme to high temperatures
additional information
the enzyme lacks an intricate network of 4 ion pairs in its 4th beta/alpha unit, (beta/alpha)4. Iintroduction of a thermophile-sourced ion pair network in the fourth beta/alpha unit of a psychophile-derived triosephosphate isomerase from Methanococcoides burtonii significantly increases its kinetic thermal stability. The enzyme with the incorporated ion pair network, shows significantly higher apparent Tm values and also displays significantly higher kinetic thermal stability
additional information
-
the enzyme lacks an intricate network of 4 ion pairs in its 4th beta/alpha unit, (beta/alpha)4. Iintroduction of a thermophile-sourced ion pair network in the fourth beta/alpha unit of a psychophile-derived triosephosphate isomerase from Methanococcoides burtonii significantly increases its kinetic thermal stability. The enzyme with the incorporated ion pair network, shows significantly higher apparent Tm values and also displays significantly higher kinetic thermal stability
additional information
-
Thermal melting of PfuTIM in buffers of different pH, overview
additional information
denaturation of the enzyme likely consists of an initial first-order reaction that forms thermally unfolded enzyme, followed by irreversibility-inducing reactions which are probably linked to aggregation of the unfolded protein
additional information
-
denaturation of the enzyme likely consists of an initial first-order reaction that forms thermally unfolded enzyme, followed by irreversibility-inducing reactions which are probably linked to aggregation of the unfolded protein
additional information
-
slow temperature-induced unfolding of yeast TIM shows three kinetic phases. A complex mechanism involving off-pathway intermediates or parallel pathways may be operating. beta-Strand-type residual structure appears below pH 8.0, and is likely to be associated with increased irreversible aggregation of the unfolded protein, which accelerates the refolding process
additional information
crystal structure represents the most thermostable triosephosphate isomerase presently known in its 3D-structure
additional information
-
crystal structure represents the most thermostable triosephosphate isomerase presently known in its 3D-structure
additional information
dimeric enzyme unfolds following a four state model denaturation process whereas monomeric variants follow a three state model
additional information
-
dimeric enzyme unfolds following a four state model denaturation process whereas monomeric variants follow a three state model