Information on EC 5.3.1.1 - Triose-phosphate isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
5.3.1.1
-
RECOMMENDED NAME
GeneOntology No.
Triose-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-Glyceraldehyde 3-phosphate = glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
show the reaction diagram
mechanism
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
show the reaction diagram
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
show the reaction diagram
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
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
show the reaction diagram
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
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
show the reaction diagram
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
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
show the reaction diagram
reaction mechanism via enediolate intermediate through proton abstraction by the catalytic base Glu167, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Calvin-Benson-Bassham cycle
-
Carbon fixation in photosynthetic organisms
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
Fructose and mannose metabolism
-
gluconeogenesis I
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
gluconeogenesis III
-
glycerol degradation to butanol
-
Glycolysis / Gluconeogenesis
-
glycolysis I (from glucose-6P)
-
glycolysis II (from fructose-6P)
-
glycolysis III (from glucose)
-
glycolysis IV (plant cytosol)
-
glycolysis V (Pyrococcus)
-
glycolysis VI (metazoan)
-
Inositol phosphate metabolism
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
sucrose degradation V (sucrose alpha-glucosidase)
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CP 25
-
-
-
-
cytoplasmic TPI
-
-
cytoplasmic triosephosphate isomerase
-
-
cytoTPI
P48491
-
D-glyceraldehyde-3-phosphate ketol-isomerase
-
-
-
-
Isomerase, triose phosphate
-
-
-
-
Lactacin B inducer protein
-
-
-
-
monoTIM
-
-
-
-
PfTIM
-
-
-
-
Phosphotriose isomerase
-
-
-
-
plastidic TPI
-
-
plastidic triosephosphate isomerase
-
-
TIM
-
-
-
-
TIM
P0A858
-
TIM
P00940
-
TIM
P60174
-
TIM
Leishmania donovani MHOM/IN/80/Dd8
Q0ZAG6
-
-
TIM
P50921
-
TIM
P62003
-
TIM
Trypanosoma brucei subsp. brucei
-
-
TIM
P52270
-
TIM
Trypanosoma cruzi T2
-
-
-
TpI
Staphylococcus aureus RN4220
-
-
-
Triose phosphate isomerase
-
-
-
-
Triose phosphate isomerase
P48491
-
Triose phosphate isomerase
-
-
Triose phosphate isomerase
Q07412
-
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
-
-
-
-
Triosephosphate isomerase
P35144
-
Triosephosphate isomerase
Bacillus megaterium DSM319
P35144
-
-
Triosephosphate isomerase
Q8L1Z5
-
Triosephosphate isomerase
Q10657
-
Triosephosphate isomerase
O02611
-
Triosephosphate isomerase
P0A858
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
P00940
-
Triosephosphate isomerase
P00943
-
Triosephosphate isomerase
P36186
-
Triosephosphate isomerase
P56076
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
P60174
-
Triosephosphate isomerase
Q0ZAG6
-
Triosephosphate isomerase
Leishmania donovani MHOM/IN/80/Dd8
Q0ZAG6
-
-
Triosephosphate isomerase
P48499
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
Q58923
-
Triosephosphate isomerase
P50921
-
Triosephosphate isomerase
P66940
-
Triosephosphate isomerase
P00939
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
Q07412
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
P62003
-
Triosephosphate isomerase
A8B3A8
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
P00942
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
Staphylococcus aureus RN4220
-
-
-
Triosephosphate isomerase
Q8MPF2
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
Q8NKN9
-
Triosephosphate isomerase
P36204
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
P04789
-
Triosephosphate isomerase
Trypanosoma brucei subsp. brucei
-
-
Triosephosphate isomerase
-
-
Triosephosphate isomerase
P52270
-
Triosephosphate isomerase
Trypanosoma cruzi T2
-
-
-
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-78-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain DSM319
SwissProt
Manually annotated by BRENDA team
Bacillus megaterium DSM319
strain DSM319
SwissProt
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
adult, recombinant enzyme
-
-
Manually annotated by BRENDA team
multiple forms of triosephosphate isomerase are the consequence of minor post-synthetic alteration(s) of form A, three major forms: A, B, C
-
-
Manually annotated by BRENDA team
isoform Tpi1
-
-
Manually annotated by BRENDA team
isoform Tpi2
SwissProt
Manually annotated by BRENDA team
ssp. Lactis IL403. Enzyme is present in high excess in wild-type cells. 10% residual activity still support more than 70% of the wild-type glycolytic flux. At at residual triosephosphate isomerase activity of 3%, dihydroxyacetone phosphate level increases four times and coincides with an increase in formate production
-
-
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/80/Dd8
-
UniProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
type II-S, commercial preparation
-
-
Manually annotated by BRENDA team
methicillin-resistant strain MRSA252
-
-
Manually annotated by BRENDA team
strain RN4220
-
-
Manually annotated by BRENDA team
Staphylococcus aureus RN4220
strain RN4220
-
-
Manually annotated by BRENDA team
bifunctional enzyme, phosphoglycerate kinase/triosephosphate isomerase
UniProt
Manually annotated by BRENDA team
brucei TIM
Uniprot
Manually annotated by BRENDA team
Trypanosoma brucei subsp. brucei
-
-
-
Manually annotated by BRENDA team
Trypanosoma cruzi T2
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
TIM deficiency is the only human glycolytic deficiency disease which is lethal, usually in early childhood. The disease symptoms concern hemolytic anemia but also neurological disorders
metabolism
-
triosephosphate isomerase is a ubiquitously distributed enzyme of the glycolysis pathway
metabolism
-
TPIs play a very important role in gluconeogenesis, fatty acid biosynthesis, pentosephosphate pathway
metabolism
-
the dimeric enzyme functions in the glycolytic pathway. In the glycolysis, the catalyzed interconversion reaction is important in the thermodynamically uphill direction of the synthesis of D-glyceraldehyde 3-phosphate
metabolism
-
the enzyme is involved in glycolysis
physiological function
-
TPI of Staphylococcus aureus is a candidate adhesion molecule for the interaction between the bacterium and the fungal pathogen Cryptococcus neoformans. TPI may recognize the mannan backbone of glucuronoxylomannan of Cryptococcus neoformans
physiological function
-, P48491
the plastid isoform of triose phosphate isomerase plays a crucial role in this transition from heterotrophic to autotrophic growth
physiological function
Staphylococcus aureus RN4220
-
TPI of Staphylococcus aureus is a candidate adhesion molecule for the interaction between the bacterium and the fungal pathogen Cryptococcus neoformans. TPI may recognize the mannan backbone of glucuronoxylomannan of Cryptococcus neoformans
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
P04789
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
Q8MPF2, -
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-, P48491
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
r
-
-
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
key reaction in glycolysis
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
the reaction is essential in vivo
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
stereospecific reaction via an enzyme-bound enediol(ate) intermediate, proton transfer from D-glyceraldehyde 3-phosphate to the carboxylate side chain of TIM Glu165, irreversible labeling with deuterium , overview
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
substrate binding perturbs residues Asn10, His95, Ser100, Glu129-Glu133, Val167-Ala186, Asn213, and Leu230-Leu126 that either are near the ligand or have direct contact with the ligand
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
TIM is highly specific for the substrates
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
triosephosphate isomerase is an enolizing enzyme, which catalyses the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
Staphylococcus aureus RN4220
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P36186
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P04789
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-, P56076
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-, Q0H294
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
Trypanosoma brucei subsp. brucei
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P50921
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P66940
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P62003
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-, Q0ZAG6
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P04789
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P36204
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
A8B3A8, -
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
Q8L1Z5
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P00943
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
Q10657
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
P0A858
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
cytoplasmic triosephosphate isomerase may be important in the glycolytic pathway for the supply of C to respiratory and biosynthetic pathways during active growth
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
Leishmania donovani MHOM/IN/80/Dd8
Q0ZAG6
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
Trypanosoma cruzi T2
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dehydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
glycerone phosphate
methylglyoxal + phosphate
show the reaction diagram
-
-
-
?
glycolaldehyde
?
show the reaction diagram
-
TIM-catalyzed reactions of glycolaldehyde are activated by phosphite dianion, kinetics, overview
-
-
?
additional information
?
-
-, Q0H294
enzyme is involved in arsenate reduction
-
-
-
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
-
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
-
-
-
additional information
?
-
-
importance of conserved residues in the vicinity of the active site that serve to position the functional K12 residue. A network of key interactions spans the interacting subunits
-
-
-
additional information
?
-
-
Plasmodium falciparum TIM is unique in possessing a Phe residue at position 96 in place of the conserved Ser that is found in TIMs from the majority of other organisms
-
-
-
additional information
?
-
-
Tau, main component of the aberrant paired helical filaments found in Alzheimer's disease, interacts with the enzyme and protects TPI against oxidative damage, overview. Interaction between Tau and triose phosphate isomerase occurs in a normal, nondisease state as well as in a neurodegeneration state
-
-
-
additional information
?
-
-
the proton transfer reaction from PGH to the Glu167 side chain, when PGH becomes sequestered in the active site, active site modeling, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
Q8MPF2, -
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-, P48491
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
key reaction in glycolysis
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
the reaction is essential in vivo
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
Staphylococcus aureus RN4220
-
-
-
-
?
additional information
?
-
-, Q0H294
enzyme is involved in arsenate reduction
-
-
-
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no metal cations are required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1Z,2Z)-N,N'-dihydroxy-4-methylcyclohexa-3,5-diene-1,2-diimine
-
-
(2E)-2-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarbothioamide
-
irreversible inhibitor
(2E)-2-[2-[(3-oxido-2,1,3-benzoxadiazol-5-yl)methoxy]benzylidene]-N-(prop-2-en-1-yl)hydrazinecarbothioamide
-
irreversible inhibitor
(2E)-N-(naphthalen-2-yl)-2-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]hydrazinecarboxamide
-
irreversible inhibitor
(2E)-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarboxamide
-
irreversible inhibitor
(4-methyl-1,2,3-thiadiazol-5-yl)methanol
-
29% inhibition at 0.4 mM
1,2,4-thiadiazole
-
59% inhibition at 0.1 mM
-
1,2,4-thiadiazole
-
-
-
1,2,6-thiadiazine
-
irreversible inhibitor
-
1,3,4-oxathiazole
-
-
-
1-Chloro-3-hydroxyacetone
-
-
2,2'-methylenebis(1,3-benzothiazole)
-
irreversible inactivation
2,2'-methylenebis(1,3-benzothiazole)
-
40% inactivation at 0.05 mM, irreversible
2,4-Dinitrofluorobenzene
-
no inhibition
2,4-Dinitrofluorobenzene
-
-
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor
2,9-dimethyl-beta-carbolinium ion
-
-
2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
-
-
2-carboxyethyl methanethiosulfonate
-
modifies four Cys per subunit of dimeric protein and induces 97% of inactivation. Inactivation does not affect secondary structure nor induce dimer dissociation. Cys modification decreases thermal stability of the enzyme
2-carboxyethylphosphonic acid
-
-
2-methyl-beta-carbolinium ion
-
-
2-phenyl-4H-chromen-4-one
-
-
2-phosphoglycerate
-
-
2-Phosphoglycolate
-
-
2-Phosphoglycolate
-
-
2-Phosphoglycolate
-
strong, competitive. Inhibition results in a large decrease in the unfolding rate constant of the protein. 2-phosphoglycolate shows similar binding affinities in the transition states for the rate-limiting steps of the forward and backward reactions, implicating that both transition states resemble each other in the active site architecture
2-Phosphoglycolate
-
competitive inhibition
2-phosphoglycolic acid
-
-
2-[(1E)-2-nitroprop-1-en-1-yl]thiophene
-
-
2-[(3-aminophenyl)disulfanyl]aniline
-
-
3,5-diphenyl-1,2,4-thiadiazole
-
74% inhibition at 0.4 mM
3-(2-benzothiazolylthio)-1-propanesulfonic acid
-
binds to the dimer interface of the enzyme and thereby abolishes its function with a high level of selectivity
3-(4-methylphenyl)-5-[(4-methylphenyl)sulfonyl]-1,2,4-thiadiazole
-
-
3-nitrobiphenyl-4-amine
-
-
3-phosphoglycerate
-
-
3-phosphoglycerate
-
binding at the active site with the dimer-interface site showing strong electrostatic anchoring of the phosphate group involving the Arg98 and Lys112 residues of TIM, comparisons of binding structures at the interface, overview
4-(4-nitrobenzylidene)-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor, 85% inhibition at 0.4 mM
4-[(5-nitrofuran-2-yl)methylidene]-4H-1,2,6-thiadiazine-3,5-diamine 1,1-dioxide
-
irreversible inhibitor
4-[(5-nitrothiophen-2-yl)methylidene]-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor
5,5'-dithio-bis(2-nitrobenzoic acid)
-
derivatizes four of the five Cys per subunit of dimeric protein, resulting in inactivation and dissociation of the dimer to stable monomers
5,5'-dithio-bis(2-nitrobenzoic acid)
A8B3A8, -
about 50% inhibition at about 0.05 mM
5,5'-dithiobis(2-nitrobenzoate)
-
no inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-[(1E)-2-nitroprop-1-en-1-yl]-1,3-benzodioxole
-
-
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
irreversible inactivation. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
91% inactivation at 0.05 mM, irreversible. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica enzyme
6,6'-bi-1,3-benzothiazole-2,2'-diamine
-
-
6-phosphogluconate
-
5 mM, 9% inhibition
6-[(E)-2-(5-nitrothiophen-2-yl)ethenyl]-2,1,3-benzoxadiazole 1-oxide
-
irreversible inhibitor
6-[(E)-2-[(4-fluorophenyl)sulfanyl]ethenyl]-2,1,3-benzoxadiazole 1-oxide
-
irreversible inhibitor
8-bromo-5,10-dioxidophenazin-2-yl chloroacetate
-
50% inhibition at 0.4 mM
Acetylphosphate
-
competitive
Acetylphosphate
-
-
AsO2-
-
competitive
AsO43-
-
competitive
ATP
-
5 mM, 39% inhibition
Atrazine
-
a herbicide which interferes with photosynthesis
bromohydroxyacetone phosphate
Q8L1Z5
suicide inhibitor
-
bromohydroxyacetone phosphate
Q10657
suicide inhibitor
-
bromohydroxyacetone phosphate
-
suicide inhibitor
-
bromohydroxyacetone phosphate
P0A858
suicide inhibitor
-
bromohydroxyacetone phosphate
-
suicide inhibitor
-
bromohydroxyacetone phosphate
P00943
suicide inhibitor
-
bromohydroxyacetone phosphate
P50921
suicide inhibitor
-
bromohydroxyacetone phosphate
P66940
suicide inhibitor
-
bromohydroxyacetone phosphate
-
suicide inhibitor
-
bromohydroxyacetone phosphate
P62003
suicide inhibitor
-
bromohydroxyacetone phosphate
-
suicide inhibitor
-
bromohydroxyacetone phosphate
P36204
suicide inhibitor
-
bromohydroxyacetone phosphate
P04789
suicide inhibitor
-
bromohydroxyacetone phosphate
-
suicide inhibitor
-
butylbrevifolin carboxylate
-
-
Chloroacetol phosphate
-
-
citrate
-
25 mM, 9% inhibition
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
-
no inhibition
cyclo(Gly-Pro-Phe-Val-Phe-PSI[CS-NH]Phe)
-
-
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
-
no inhibition
cyclo[Trp-Phe-D-Pro-Phe-Phe-Lys(benzyloxycarbonyl)-]
-
-
cyclo[Trp-Tyr(OSO3Na)-D-Phe-Thr(OSO3Na)-Lys(benzyloxycarbonyl)-]
-
noncompetitive, reversible
D-alpha-glycerophosphate
-
competitive
D-alpha-glycerophosphate
-
-
D-alpha-glycerophosphate
-
competitive
D-alpha-glycerophosphate
-
competitive
D-erythrose 4-phosphate
-
-
DL-glycidol phosphate
Q8L1Z5
suicide inhibitor
-
DL-glycidol phosphate
Q10657
suicide inhibitor
-
DL-glycidol phosphate
-
suicide inhibitor
-
DL-glycidol phosphate
P0A858
suicide inhibitor
-
DL-glycidol phosphate
-
suicide inhibitor
-
DL-glycidol phosphate
P00943
suicide inhibitor
-
DL-glycidol phosphate
P50921
suicide inhibitor
-
DL-glycidol phosphate
P66940
suicide inhibitor
-
DL-glycidol phosphate
-
suicide inhibitor
-
DL-glycidol phosphate
P62003
suicide inhibitor
-
DL-glycidol phosphate
-
suicide inhibitor
-
DL-glycidol phosphate
P36204
suicide inhibitor
-
DL-glycidol phosphate
P04789
suicide inhibitor
-
DL-glycidol phosphate
-
suicide inhibitor
-
ethyl 3-(3,5-di-tert-butyl-4-hydroxyphenyl)-1,2,4-thiadiazole-5-carboxylate
-
-
ethyl 3-phenyl-1,2,4-thiadiazole-5-carboxylate
-
-
ethylbrevifolin carboxylate
-
-
fluorodifen
-
a herbicide which interferes with photosynthesis
fructose 1,6-diphosphate
-
5 mM, 69% inhibition
fructose 6-phosphate
-
5 mM, 44% inhibition
glucose 1-phosphate
-
5 mM, 10% inhibition
glucose 6-phosphate
-
5 mM, 25% inhibition
glycerol 1-phosphate
-
-
GSSG
-
oxidized glutathione is a strong inhibitor of the enzyme at low concentrations
iodoacetamide
-
-
iodoacetate
-
no inhibition
iodoacetate
-
-
KFGNGSYTGEVS
-
peptide that corresponds to loop 3 of the triosephosphate isomerase, residues 68-79. Efficient inhibitor with the activity falling to about 45% at 1000fold molar excess of the peptide in case of the wild-type enzyme. In the case of either of the mutants, Y74C and Y74G, even at 100fold molar excess of the peptide, only 30% activity can be obtained
KYGNGSCTGEVS
-
peptide that is an analog of the peptide that corresponds to loop 3 of the protein, residues 68-79, with the replacement Y74C and F69Y. Inhibits the activity of the mutant enzymes Y74C and Y74G, with about 40% activity remaining in the presence of 1000fold molar excess of the peptide
Mannotriose
-
docking simulation
methyl methanethiosulfonate
-
derivatizes Cys14 to a methyl sulfide
methyl methanethiosulfonate
-
no inhibition
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
no inhibition
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
the sensitivity of enzyme from Trypanosoma cruzi is about 40times higher than that of Trypanosoma brucei and 200times higher than that of Leishmania mexicana
methyl methanethiosulfonate
-
derivatizes three of the five Cys per subunit of dimeric protein and induces 50% of inactivation. Inactivation does not affect secondary structure nor induce dimer dissociation. Cys modification decreases thermal stability of the enzyme
methyl methanethiosulfonate
A8B3A8, -
about 50% inhibition at about 0.05 mM
methylbrevifolin carboxylate
-
molecular docking simulations and enzyme binding structure, and inhibition kinetics, overview
methylmethane thiosulfonate
-
0.6 mM, 2 h, complete loss of activity, dissociates the dimeric enzyme inducing formation of a compact monomeric state
N-[(2-oxido-4-phenyl-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
-
72% inhibition at 0.4 mM
N-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
-
41% inhibition at 0.4 mM
o-Iodosobenzoate
-
-
p-benzoquinone
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
PCMB
-
no inhibition
phenazine 5,9-dioxide
-
84% inhibition at 0.4 mM
-
phosphate
-
competitive
phosphate
-
competitive, occupies the substrate binding pocket
phosphoenolpyruvate
-
competitive
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
Phosphoglycolate
-
competitive
Phosphoglycolate
-
-
Phosphoglycolate
-
competitive
Phosphoglycolate
-
and its corresponding hydroxamate; competitive
Phosphoglycolate
-
-
Phosphoglycolate
-
2-phosphoglycolate
Phosphoglycolate
-
-
Phosphoglycolate
-
2-phosphoglycolate
Phosphoglycolate
-
2-phosphoglycolate
phosphoglycoloaldoxime
-
-
phosphoglycolohydrazide
-
-
Phosphoglycolohydroxamate
-
-
Phosphoglycolohydroxamate
-
-
Phosphoglycolohydroxamate
-
the reaction-intermediate analogue binds to the active site with two hydrogen-bonding interactions between PGH and the Glu167 side-chain oxygen atoms
S-Phenyl-p-toluenethiosulfonate
-
no inhibition
S-Phenyl-p-toluenethiosulfonate
-
-
S-Phenyl-p-toluenethiosulfonate
-
no inhibition
S-Phenyl-p-toluenethiosulfonate
-
-
SO42-
-
CuSO4
succinate
-
5 mM, 9% inhibition
[3-amino-3-(hydroxyimino)propyl]phosphonic acid
-
-
methylmethane thiosulfonate
-
modification at C15 in the dimer interface, inducing abolition of catalysis and structural changes. Susceptibility of Trypanosoma cruzi enzyme to modification of C15 is nearly 100fold higher than susceptibility of C15 of Trypanosoma brucei
additional information
-
ANWKCNGTLE, the peptide that corresponds to loop 1 of triosephosphate isomerase, residues 9-18, shows only negligible inhibition of wild-type enzyme and mutant enzymes Y74G and Y74C, with a fall in the enzymatic activity by only about 20% at 1000fold molar excess of the peptide
-
additional information
-
in drug-resistant SGC7901 cells induced by vincristine sulfate, triosephosphate isomerase is downregulated.The sensitivity of TPI-SGC7901/VCR cells to adriamycin, vincristine, 5-fluorouracil and cis-dichlorodiamine platinum, as well as the accumulation and retention to adriamycin, are significantly increased when compared to their control cell lines
-
additional information
-
brevifolin carboxylate derivatives isolated from Geranium bellum selectively inactivate the enzyme partially, no inhibition by methyl tri-O-methylbrevifolin carboxylate
-
additional information
-
stronger inhibition by alpha-(1,3)-mannooligosaccharides than with triose, binding constants, overview
-
additional information
-
recombinant expression of Tau in CHO-K1 cells leads to increased protection of TPI against oxidative damage, but also to decreased enzyme activity, with unaltered TPI expression levels
-
additional information
-
TPI phosphorylation by cyclin A/Cdk2 kinase leads to reduced TPI activity, prevented by treatment with olomoucine, a specific inhibitor of Cdk2
-
additional information
-
not inhibited by 1,2,6-thiadiazine, phenazine 5,9-dioxide, and 1,3,4-oxathiazole
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9-methyl-beta-carbolinium ion
-
1 mM, stimulates
phosphite
Trypanosoma brucei subsp. brucei
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.084
-
D-glyceraldehyde 3-phosphate
-
22C, pH 7.6
0.14
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/A73C, 25C, pH 7.4
0.16
-
D-glyceraldehyde 3-phosphate
-
mutant P168A, 25C, pH 7.6
0.18
-
D-glyceraldehyde 3-phosphate
-
mutant E168D, pH 7.4, 25C
0.19
-
D-glyceraldehyde 3-phosphate
-
recombinant wild-type enzyme
0.2
-
D-glyceraldehyde 3-phosphate
-
active form P2 of TIM, at 25C, pH 7.4
0.22
-
D-glyceraldehyde 3-phosphate
-
plastidic triosephosphate isomerase
0.24
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme S227A
0.25
-
D-glyceraldehyde 3-phosphate
-
isoenzyme A
0.25
-
D-glyceraldehyde 3-phosphate
-
D-glyceraldehyde 3-phosphate
0.25
-
D-glyceraldehyde 3-phosphate
P04789
wild-type enzyme
0.25
-
D-glyceraldehyde 3-phosphate
Trypanosoma brucei subsp. brucei
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25C
0.26
-
D-glyceraldehyde 3-phosphate
-
wild-type, 25C, pH 7.6
0.26
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.6, 25C
0.28
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme S227N
0.28
-
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25C
0.28
-
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25C
0.28
-
D-glyceraldehyde 3-phosphate
-
mutant W162F
0.29
-
D-glyceraldehyde 3-phosphate
-
cytoplasmic triosephosphate isomerase
0.3
-
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
0.3
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, mutant enzyme C126S
0.3
-
D-glyceraldehyde 3-phosphate
-, Q0H294
pH 8.0, 25C
0.3
-
D-glyceraldehyde 3-phosphate
-
active form P1 of TIM, at 25C, pH 7.4
0.31
-
D-glyceraldehyde 3-phosphate
-
-
0.31
-
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma cruzi, pH 7.4, 25C
0.31
-
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25C
0.31
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.32
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14T
0.33
-
D-glyceraldehyde 3-phosphate
-
isoenzyme B
0.33
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14P
0.33
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme Y74C
0.34
-
D-glyceraldehyde 3-phosphate
-
enzyme form I
0.34
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme Y74G
0.34
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme R191S
0.35
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, wild-type enzyme
0.35
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
0.35
-
D-glyceraldehyde 3-phosphate
-
-
0.35
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/S71C, 25C, pH 7.4
0.35
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25C
0.35
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
0.35
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.38
-
D-glyceraldehyde 3-phosphate
-
wild-type, 25C, pH 7.4
0.39
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
0.4
-
D-glyceraldehyde 3-phosphate
-
-
0.4067
-
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
0.42
-
D-glyceraldehyde 3-phosphate
-
-
0.42
-
D-glyceraldehyde 3-phosphate
-
-
0.42
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14V
0.42
-
D-glyceraldehyde 3-phosphate
-
mutant C15A, pH 7.4, 25C
0.42
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.43
-
D-glyceraldehyde 3-phosphate
-
enzyme form II
0.43
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14A
0.43
-
D-glyceraldehyde 3-phosphate
-
mutant W196F
0.44
-
D-glyceraldehyde 3-phosphate
-
-
0.45
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
0.46
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
0.47
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, wild-type enzyme
0.47
-
D-glyceraldehyde 3-phosphate
A8B3A8, -
in 100 mM triethanolamine, pH 7.4, at 25C
0.48
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/S79C, 25C, pH 7.4
0.5
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14S
0.5
-
D-glyceraldehyde 3-phosphate
-
mutant C14S, 25C, pH 7.4
0.5
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25C
0.53
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, dimeric enzyme form
0.55
-
D-glyceraldehyde 3-phosphate
-
enzyme form III
0.6
-
D-glyceraldehyde 3-phosphate
-
cytosolic enzyme
0.6
-
D-glyceraldehyde 3-phosphate
-
D-glyceraldehyde 3-phosphate
0.6
-
D-glyceraldehyde 3-phosphate
-
mutant F12W
0.61
-
D-glyceraldehyde 3-phosphate
-
mutant A178L, pH 7.6, 25C
0.62
-
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25C
0.62
-
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25C
0.68
-
D-glyceraldehyde 3-phosphate
-
chloroplastic enzyme
0.69
-
D-glyceraldehyde 3-phosphate
-
mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25C
0.69
-
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25C
0.73
-
D-glyceraldehyde 3-phosphate
-
mutant W75F/W162F/W196F
0.74
-
D-glyceraldehyde 3-phosphate
-
mutant W75F
0.75
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/A69C, 25C, pH 7.4
0.78
-
D-glyceraldehyde 3-phosphate
-
wildtype
0.8
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, mutant enzyme C126A
0.8
-
D-glyceraldehyde 3-phosphate
-
-
0.84
-
D-glyceraldehyde 3-phosphate
-
pH 7.0, 25C
0.87
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, tetrameric enzyme form
0.9
-
D-glyceraldehyde 3-phosphate
-
-
0.91
-
D-glyceraldehyde 3-phosphate
-
mutant D225Q, pH 7.4, 25C
0.94
-
D-glyceraldehyde 3-phosphate
-
mutant W173F
0.97
-
D-glyceraldehyde 3-phosphate
-
presence of methyl methanethiosulfonate
1
-
D-glyceraldehyde 3-phosphate
-
mutant W162F/W173F/W196F
1
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
1.03
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
1.09
-
D-glyceraldehyde 3-phosphate
-
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25C
1.1
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme R191A
1.1
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7., wild-type enzyme
1.1
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25C
1.12
-
D-glyceraldehyde 3-phosphate
-
mutant W75F/W162F/W173F
1.13
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
1.2
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G
1.2
-
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25C
1.2
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96W
1.2
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25C
1.2
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
1.26
-
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25C
1.27
-
D-glyceraldehyde 3-phosphate
-
-
1.4
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
1.4
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
1.5
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23C; mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
1.9
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme; wild-type enzyme
1.9
-
D-glyceraldehyde 3-phosphate
-
mutant W75F/W173F/W196F
2.18
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96S
2.44
-
D-glyceraldehyde 3-phosphate
-
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25C
2.49
-
D-glyceraldehyde 3-phosphate
-
mutant D213A, pH 7.5, 25C
2.62
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96H
3.27
-
D-glyceraldehyde 3-phosphate
-
mutant D213Q, pH 7.5, 25C
3.3
-
D-glyceraldehyde 3-phosphate
-
monomeric mutant A178L, pH 7.6, 25C
3.46
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.5, 25C
3.56
-
D-glyceraldehyde 3-phosphate
-
mutant K183S, pH 7.5, 25C
3.6
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14F
3.7
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, mutant enzyme K174G/T175G/A176G
3.8
-
D-glyceraldehyde 3-phosphate
-
monomeric wild-type, pH 7.6, 25C
4
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
4.8
-
D-glyceraldehyde 3-phosphate
-
mutant A238S; pH 7.6, mutant enzyme A238S
8.6
-
D-glyceraldehyde 3-phosphate
-
presence of 2-carboxyethyl methanethiosulfonate
9.09
-
D-glyceraldehyde 3-phosphate
-
mutant K183A, pH 7.5, 25C
50
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25C
0.5
-
dihydroxyacetone phosphate
-
mutant P168A, 25C, pH 7.6
0.6
-
dihydroxyacetone phosphate
-
25C, pH 7.4, mutant enzyme C126S
0.7
-
dihydroxyacetone phosphate
Trypanosoma brucei subsp. brucei
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25C
0.9
-
dihydroxyacetone phosphate
-
wild-type, 25C, pH 7.6
0.9
-
dihydroxyacetone phosphate
-
wild-type, pH 7.6, 25C
0.97
-
dihydroxyacetone phosphate
-
30C, pH 7.6, wild-type enzyme
1.1
-
dihydroxyacetone phosphate
-
25C, pH 7.4, dimeric enzyme form
1.4
-
dihydroxyacetone phosphate
-
mutant A178L, pH 7.6, 25C
2.1
-
dihydroxyacetone phosphate
-
25C, pH 7.4, wild-type enzyme
7.6
-
dihydroxyacetone phosphate
-
monomeric wild-type, pH 7.6, 25C
9.3
-
dihydroxyacetone phosphate
-
monomeric mutant A178L, pH 7.6, 25C
11
-
dihydroxyacetone phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G
15
-
dihydroxyacetone phosphate
-
30C, pH 7.6, mutant enzyme K174G/T175G/A176G
18
-
dihydroxyacetone phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
0.26
-
glycerone phosphate
-
isoenzyme B
0.37
-
glycerone phosphate
-
isoenzyme A
0.59
-
glycerone phosphate
-
-
0.67
-
glycerone phosphate
P04789
mutant enzyme R191A
0.69
-
glycerone phosphate
-
enzyme form III
0.7
-
glycerone phosphate
P04789
mutant enzyme D227N
0.75
-
glycerone phosphate
-
-
0.82
-
glycerone phosphate
-
enzyme form II
0.88
-
glycerone phosphate
-
-
0.9
-
glycerone phosphate
P04789
mutant enzyme D227A
1
-
glycerone phosphate
P04789
wild-type enzyme
1.1
-
glycerone phosphate
-
recombinant wild-type enzyme
1.1
-
glycerone phosphate
-
glycerone phosphate
1.2
-
glycerone phosphate
-
-
1.23
-
glycerone phosphate
-
-
1.3
-
glycerone phosphate
-
recombinant enzyme
1.5
-
glycerone phosphate
-
enzyme form I
1.5
-
glycerone phosphate
-
glycerone phosphate, cytosolic enzyme
1.6
-
glycerone phosphate
P04789
mutant enzyme R191S
2.5
-
glycerone phosphate
-
chloroplastic enzyme
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.25
-
D-glyceraldehyde 3-phosphate
-
monomeric mutant A178L, pH 7.6, 25C
0.6
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25C
0.69
-
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25C
1
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25C
1.04
-
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25C
1.7
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
1.9
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14F
2.2
-
D-glyceraldehyde 3-phosphate
-
monomeric wild-type, pH 7.6, 25C
4.2
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25C
11
-
D-glyceraldehyde 3-phosphate
-
mutant E168D, pH 7.4, 25C
60
-
D-glyceraldehyde 3-phosphate
-
mutant P168A, 25C, pH 7.6
67
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme Y74G
160
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
185
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96H
190
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
240
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G
261
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, mutant enzyme K174G/T175G/A176G
330
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
483
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/A73C, 25C, pH 7.4
600
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
620
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96S
750
-
D-glyceraldehyde 3-phosphate
-
mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25C
750
-
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25C
750
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
770
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
833
-
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25C
833
-
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25C
1100
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, mutant enzyme C126S
1367
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
1470
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.5, 25C
1570
-
D-glyceraldehyde 3-phosphate
-
mutant D213A, pH 7.5, 25C
1600
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme S227N
1666
-
D-glyceraldehyde 3-phosphate
-
presence of 2-carboxyethyl methanethiosulfonate
1830
-
D-glyceraldehyde 3-phosphate
-
mutant D213Q, pH 7.5, 25C
2000
-
D-glyceraldehyde 3-phosphate
-
mutant K183S, pH 7.5, 25C
2100
-
D-glyceraldehyde 3-phosphate
Trypanosoma brucei subsp. brucei
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25C
2170
-
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25C
2170
-
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25C
2330
-
D-glyceraldehyde 3-phosphate
-
mutant K183A, pH 7.5, 25C
2417
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme Y74C
2420
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme Y74C
2450
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, tetrameric enzyme form
2466
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96W
2500
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzymeR191A
2600
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme S227A
2600
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/A69C, 25C, pH 7.4
2670
-
D-glyceraldehyde 3-phosphate
-
mutant C15A, pH 7.4, 25C
2967
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/S79C, 25C, pH 7.4
3100
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, mutant enzyme C126A
3166
-
D-glyceraldehyde 3-phosphate
-
mutant W162F/W173F/W196F
3166
-
D-glyceraldehyde 3-phosphate
-
presence of methyl methanethiosulfonate
3200
-
D-glyceraldehyde 3-phosphate
-
mutant C14S/S71C, 25C, pH 7.4
3333
-
D-glyceraldehyde 3-phosphate
-
mutant W162F
3570
-
D-glyceraldehyde 3-phosphate
-
wild-type, 25C, pH 7.6
3666
-
D-glyceraldehyde 3-phosphate
-
mutant W75F/W162F/W173F
3667
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14P
3670
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14P
3830
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14T
3833
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14T
4000
-
D-glyceraldehyde 3-phosphate
-
-
4000
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14V
4000
-
D-glyceraldehyde 3-phosphate
P04789
mutant enzyme R191S
4160
-
D-glyceraldehyde 3-phosphate
-
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25C
4166
-
D-glyceraldehyde 3-phosphate
-
mutant W196F
4170
-
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
4183
-
D-glyceraldehyde 3-phosphate
-
wild-type, 25C, pH 7.4
4300
-
D-glyceraldehyde 3-phosphate
-
30C, pH 7.6, wild-type enzyme
4300
-
D-glyceraldehyde 3-phosphate
-
pH 7.0, 25C
4300
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25C
4300
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
4330
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, wild-type enzyme
4333
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, wild-type enzyme
4333
-
D-glyceraldehyde 3-phosphate
-
mutant W75F/W173F/W196F
4400
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.6, 25C
4467
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
4467
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
4470
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
4500
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
4600
-
D-glyceraldehyde 3-phosphate
-
mutant D225Q, pH 7.4, 25C
4667
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant enzyme A238S
4670
-
D-glyceraldehyde 3-phosphate
-
mutant A238S; pH 7.6, mutant enzyme A238S
4700
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7., wild-type enzyme
4833
-
D-glyceraldehyde 3-phosphate
-
25C, pH 7.4, dimeric enzyme form
5000
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14S
5000
-
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma cruzi, pH 7.4, 25C
5000
-
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25C
5133
-
D-glyceraldehyde 3-phosphate
-
mutant C14S, 25C, pH 7.4
5167
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14A
5170
-
D-glyceraldehyde 3-phosphate
-
pH 7.4, 25C, mutant enzyme C14A
5170
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
5300
-
D-glyceraldehyde 3-phosphate
-
mutant A178L, pH 7.6, 25C
5500
-
D-glyceraldehyde 3-phosphate
-
mutant F12W
6000
-
D-glyceraldehyde 3-phosphate
-
recombinant enzyme
6000
-
D-glyceraldehyde 3-phosphate
P04789
wild-type enzyme
6166
-
D-glyceraldehyde 3-phosphate
-
mutant W173F
6170
-
D-glyceraldehyde 3-phosphate
-
-
6400
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
6900
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.4, 25C
7000
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme; wild type enzyme
7020
-
D-glyceraldehyde 3-phosphate
-
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25C
7166
-
D-glyceraldehyde 3-phosphate
-
mutant W75F/W162F/W196F
7300
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25C
7666
-
D-glyceraldehyde 3-phosphate
-
wildtype
7666
-
D-glyceraldehyde 3-phosphate
-
-
8000
-
D-glyceraldehyde 3-phosphate
-
mutant W75F
8670
-
D-glyceraldehyde 3-phosphate
-
-
9000
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
14670
-
D-glyceraldehyde 3-phosphate
-
wild-type, pH 7.5, 25C
15670
-
D-glyceraldehyde 3-phosphate
-
mutant D213A, pH 7.5, 25C
16700
-
D-glyceraldehyde 3-phosphate
-
-
18330
-
D-glyceraldehyde 3-phosphate
-
mutant D213Q, pH 7.5, 25C
20000
-
D-glyceraldehyde 3-phosphate
-
mutant K183S, pH 7.5, 25C
23330
-
D-glyceraldehyde 3-phosphate
-
mutant K183A, pH 7.5, 25C
42330
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
68330
-
D-glyceraldehyde 3-phosphate
-
22C, pH 7.6
0.06
-
dihydroxyacetone phosphate
-
monomeric mutant A178L, pH 7.6, 25C
0.25
-
dihydroxyacetone phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
0.8
-
dihydroxyacetone phosphate
-
monomeric wild-type, pH 7.6, 25C
19
-
dihydroxyacetone phosphate
-
mutant P168A, 25C, pH 7.6
50
-
dihydroxyacetone phosphate
-
30C, pH 7.6, mutant enzyme V167G/W168G
54
-
dihydroxyacetone phosphate
-
30C, pH 7.6, mutant enzyme K174G/T175G/A176G
60
-
dihydroxyacetone phosphate
-
25C, pH 7.4, mutant enzyme C126S
267
-
dihydroxyacetone phosphate
-
25C, pH 7.4, dimeric enzyme form
300
-
dihydroxyacetone phosphate
Trypanosoma brucei subsp. brucei
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25C
430
-
dihydroxyacetone phosphate
-
30C, pH 7.6, wild-type enzyme
500
-
dihydroxyacetone phosphate
-
25C, pH 7.4, wild-type enzyme
500
-
dihydroxyacetone phosphate
-
mutant A178L, pH 7.6, 25C
645
-
dihydroxyacetone phosphate
-
wild-type, 25C, pH 7.6
800
-
dihydroxyacetone phosphate
-
wild-type, pH 7.6, 25C
63
-
glycerone phosphate
P04789
mutant enzyme R191A
180
-
glycerone phosphate
P04789
mutant enzyme D227A
200
-
glycerone phosphate
P04789
mutant enzyme D227N
240
-
glycerone phosphate
P04789
mutant enzyme R191S
367
-
glycerone phosphate
-
-
1000
-
glycerone phosphate
-
recombinant enzyme
1000
-
glycerone phosphate
P04789
wild-type enzyme
1080
-
glycerone phosphate
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25C
9226
0.9
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25C
9226
28.5
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96S
9226
70.5
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96H
9226
84
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25C
9226
120
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
9226
160
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
9226
280
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
9226
520
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
9226
540
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
9226
1933
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
9226
2050
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, mutant F96W
9226
3250
-
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
9226
5119
-
D-glyceraldehyde 3-phosphate
-
pH 7.0, 25C
9226
6600
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25C
9226
8400
-
D-glyceraldehyde 3-phosphate
Trypanosoma brucei subsp. brucei
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25C
9226
10850
-
D-glyceraldehyde 3-phosphate
-
pH 7.6, wild-type enzyme
9226
12000
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23C
9226
12200
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25C
9226
12750
-
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
9226
430
-
dihydroxyacetone phosphate
Trypanosoma brucei subsp. brucei
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25C
9850
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05
-
2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
-
-
0.019
-
2-Phosphoglycolate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25C
0.024
-
2-Phosphoglycolate
-
wild-type enzyme
0.043
-
2-Phosphoglycolate
-
25C, pH 7.4, dimeric enzyme form
0.05
-
2-Phosphoglycolate
-
wild-type, 25C, pH 7.6
0.05
-
2-Phosphoglycolate
-
wild-type, pH 7.6, 25C
0.076
-
2-Phosphoglycolate
-
mutant enzyme C14F
0.17
-
2-Phosphoglycolate
-
monomeric mutant A178L, pH 7.6, 25C
0.3
-
2-Phosphoglycolate
-
mutant P168A, 25C, pH 7.6
0.39
-
2-Phosphoglycolate
-
mutant A178L, pH 7.6, 25C
1.1
-
2-Phosphoglycolate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25C
6
-
2-Phosphoglycolate
-
-
89
-
2-Phosphoglycolate
-
pH 7.6, wild-type enzyme
101
-
2-Phosphoglycolate
-
pH 7.6, mutant enzyme A238S
1.9
-
3-phosphoglycerate
-
pH 7.6, wild-type enzyme
5
-
3-phosphoglycerate
-
above, pH 7.6, mutants F96W, F96S, and F96H
11
-
arsenate
-
30C, pH 7.6, wild-type enzyme
29
-
arsenate
-
30C, pH 7.6, mutant enzyme K174G/T175G/A176G
30
-
arsenate
-
30C, pH 7.6, mutant enzyme V167G/W168G
31
-
arsenate
-
30C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
4.9
-
AsO43-
-
wild-type, 25C, pH 7.6
4.9
-
AsO43-
-
wild-type, pH 7.6, 25C
5.1
-
AsO43-
-
monomeric wild-type, pH 7.6, 25C
5.8
-
AsO43-
-
mutant P168A, 25C, pH 7.6
7.8
-
AsO43-
-
mutant A178L, pH 7.6, 25C
17.9
-
AsO43-
-
monomeric mutant A178L, pH 7.6, 25C
1.8
-
glycerol 1-phosphate
-
-
0.0034
-
phosphoglycoloaldoxime
-
-
0.111
-
phosphoglycolohydrazide
-
-
0.003
-
Phosphoglycolohydroxamate
-
-
0.159
-
[3-amino-3-(hydroxyimino)propyl]phosphonic acid
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
(1Z,2Z)-N,N'-dihydroxy-4-methylcyclohexa-3,5-diene-1,2-diimine
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
(2E)-2-[(4-methyl-5-oxido-1,2,5-oxadiazol-3-yl)methylidene]hydrazinecarbothioamide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
(2E)-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarbothioamide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
(2E)-2-[2-[(3-oxido-2,1,3-benzoxadiazol-5-yl)methoxy]benzylidene]-N-(prop-2-en-1-yl)hydrazinecarbothioamide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
(2E)-N-(naphthalen-2-yl)-2-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]hydrazinecarboxamide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.03
0.1
(2E)-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-[(5-nitrofuran-2-yl)methylidene]hydrazinecarboxamide
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.0035
-
1,2,4-thiadiazole
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
-
0.013
-
1,2,6-thiadiazine
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
-
0.01
-
1,3,4-oxathiazole
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
-
0.03
0.1
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
2-phenyl-4H-chromen-4-one
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
2-[(1E)-2-nitroprop-1-en-1-yl]thiophene
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
3,5-diphenyl-1,2,4-thiadiazole
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
3-(4-methylphenyl)-5-[(4-methylphenyl)sulfonyl]-1,2,4-thiadiazole
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
3-nitrobiphenyl-4-amine
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
4-(4-nitrobenzylidene)-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.02
-
4-[(5-nitrofuran-2-yl)methylidene]-4H-1,2,6-thiadiazine-3,5-diamine 1,1-dioxide
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
4-[(5-nitrothiophen-2-yl)methylidene]-2,6-bis(2-phenylethyl)-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
5-[(1E)-2-nitroprop-1-en-1-yl]-1,3-benzodioxole
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.03
0.1
6-[(E)-2-(5-nitrothiophen-2-yl)ethenyl]-2,1,3-benzoxadiazole 1-oxide
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.1
-
6-[(E)-2-[(4-fluorophenyl)sulfanyl]ethenyl]-2,1,3-benzoxadiazole 1-oxide
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.4
-
8-bromo-5,10-dioxidophenazin-2-yl chloroacetate
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.014
-
butylbrevifolin carboxylate
-
-
0.1
-
ethyl 3-(3,5-di-tert-butyl-4-hydroxyphenyl)-1,2,4-thiadiazole-5-carboxylate
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.03
0.1
ethyl 3-phenyl-1,2,4-thiadiazole-5-carboxylate
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.008
-
ethylbrevifolin carboxylate
-
-
0.0066
-
methylbrevifolin carboxylate
-
-
0.1
-
N-[(2-oxido-4-phenyl-1,2,5-oxadiazol-3-yl)methyl]naphthalen-1-amine
-
IC50 about 0.1 mM, in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
0.026
-
phenazine 5,9-dioxide
-
in 100 mM triethanolamine, 10 mM EDTA, pH 7.4 and 10% of dimethyl sulfoxide, at 36C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2397
-
-
-
2500
-
-
recombinant wild-type enzyme
3183
-
-
-
3527
-
-
-
5360
-
-
isoenzyme A
5700
-
-
22C, pH 7.6
6900
-
-
isoenzyme B
8060
-
-
-
10240
-
-
-
13000
-
-
purified native enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
specific activity of wild-type and mutant enzymes Y74C and Y74G
additional information
-
-
quantitative TIM-catalyzed isomerization of D-glyceraldehyde 3-phosphate to form glycerone phosphate is coupled to the oxidation of NADH using glycerol 3-phosphate dehydrogenase
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
8.7
-
-
6.8
8.8
-
-
7
9.5
-
-
7
-
-
assay at
7.2
7.5
-
cytosolic enzyme
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
assay at
7.6
-
-
assay at
7.6
-
-
assay at
8
-
Q8L1Z5
optimum is near pH 8.0
8
-
Q10657
optimum is near pH 8.0
8
-
-
optimum is near pH 8.0
8
-
P0A858
optimum is near pH 8.0
8
-
-
optimum is near pH 8.0
8
-
P00943
optimum is near pH 8.0
8
-
P50921
optimum is near pH 8.0
8
-
P66940
optimum is near pH 8.0
8
-
-
optimum is near pH 8.0
8
-
P62003
optimum is near pH 8.0
8
-
P36204
optimum is near pH 8.0
8
-
P04789
optimum is near pH 8.0
8
-
-
optimum is near pH 8.0
8.4
-
-
chloroplastic enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6.0: about 60% of maximal activity, pH 9.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
33
40
-
cytosolic enzyme
35
-
-
assay at
37
-
-
assay at
50
-
-
chloroplastic enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
45
-
20C: about 65% of maximal activity, 45C: about 20% of maximal activity, cytosolic enzyme
25
50
-
for the wild type enzyme, there is an increase in activity over the temperature range 25-40C, with a leveling off between 40C and 50C
35
53
-
35C: about 25% of maximal activity, 53C: about 70% of maximal activity, chloroplastic enzyme
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
-
-
recombinant His6-tagged enzyme
7.7
-
A8B3A8, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
immature, cytoplasmic triosephosphate isomerase
Manually annotated by BRENDA team
-
colocalization of triose phosphate isomerase and tau-crystallin in corneal epithelium. High accumulation of both proteins starts in the late embryonic development with maximum expression in a two-week post-hatched animal
Manually annotated by BRENDA team
-
fresh fruit without peel and stone
Manually annotated by BRENDA team
-
levels of cytoplasmic triosephosphate isomerase protein decrease with tissue age. Expanding leaves have the highest ratio of cytoplasmic triosephosphate isomerase to plastidic triosephosphate isomerase
Manually annotated by BRENDA team
-
cardiac; skeletal
Manually annotated by BRENDA team
-
skeletal
Manually annotated by BRENDA team
-
breast muscle
Manually annotated by BRENDA team
-
gastric cancer cell
Manually annotated by BRENDA team
-
gradient of triosephosphate isomerase along the shoot axis with the highest levels in youngest tissues
Manually annotated by BRENDA team
additional information
-
isoenzyme B is found in most differentiated tissues, isoenzyme A is found in lymphoblasts, fibroblasts, and certain neoplastic tissues. The two isoenzymes are the result of two independent cistrons
Manually annotated by BRENDA team
additional information
-
cytoplasmic triosephosphate isomerase is barely detectable in immature ovaries, sepals and petals
Manually annotated by BRENDA team
additional information
-
the enzyme expression is upregulated in lung squamous cell carcinoma, correlated with peroxiredoxin 6 upregulation, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Staphylococcus aureus RN4220
-
-
-
Manually annotated by BRENDA team
-, P48491
with plastid TPI isozyme
Manually annotated by BRENDA team
-
the enzymes glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase and aldolase are located close to one another in the pea leaf chloroplast stroma. Aldolase is located close to sedoheptulose bisphosphatase
Manually annotated by BRENDA team
-
analysis of the TPI import signal
Manually annotated by BRENDA team
-
expression of the soluble recombinant enzyme in Escherichia coli
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bartonella henselae (strain ATCC 49882 / Houston 1)
Brucella melitensis biotype 2 (strain ATCC 23457)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Coccidioides immitis (strain RS)
Cryptosporidium parvum (strain Iowa II)
Escherichia coli (strain K12 / DH10B)
Escherichia coli (strain K12 / MC4100 / BW2952)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Leishmania sp. 'siamensis'
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
mutant enzyme C14T, gel filtration
22000
25360
-
genetically engineered monomeric enzyme form, gel filtration, sedimentation equilibrium experiments
44800
-
-
recombinant enzyme, gel filtration
50000
53000
-
cytosolic enzyme, gel filtration, sucrose density gradient centrifugation
50000
-
-
gel filtration
53000
-
-
equilibrium ultracentrifugation
53000
-
-
gel filtration, both wild-type and mutant M80T
53260
-
-
calculation from primary structure
53300
-
-
gel filtration
54000
-
-
chloroplastic enzyme, gel filtration, sucrose density gradient centrifugation
54000
-
-
gel filtration
54000
-
-
gel filtration
55000
-
-
dimer, gel filtration
56000
-
-
gel filtration
56000
-
-
gel filtration
56000
-
-
sucrose density gradient centrifugation, equilibrium ultracentrifugation
56000
-
-
gel filtration
60250
-
-
gel filtration
66000
-
-
SDS-PAGE after UV cross-linking
108000
-
-
tetramer, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 26500, SDS-PAGE
?
-
x * 27000, SDS-PAGE; x * 27832, electrospray mass spectrometry
?
-
x * 27000, SDS-PAGE
?
-
x * 28000, SDS-PAGE
?
-, Q0H294
x * 43000, SDS-PAGE
?
-
x * 30000, about, SDS-PAGE
?
-, Q0ZAG6
x * 27600, SDS-PAGE
?
Leishmania donovani MHOM/IN/80/Dd8
-
x * 27600, SDS-PAGE
-
?
Staphylococcus aureus RN4220
-
x * 30000, about, SDS-PAGE
-
dimer
-
2 * 27000, SDS-PAGE
dimer
-
two types of subunits possess similar but distinguishable amino acid composition, 3 electrophorectic forms: AA, AB, BB
dimer
-
each subunit contains an active site
dimer
-
primary structure of subunit
dimer
-
2 * 26500-27300, SDS-PAGE, subunit composition of the three forms A, B, and C is alpha2, alpha,beta, and beta2
dimer
-
2 * 27000, SDS-PAGE of denatured cytosolic enzyme
dimer
-
2 * 26500, cytosolic enzyme, SDS-PAGE; 2 * 27000, chloroplastic enzyme, SDS-PAGE
dimer
-
2 * 28000, SDS-PAGE
dimer
-
2 * 27244, calculation from nucleotide sequence
dimer
-
wild-type enzyme consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit
dimer
-
the low stability of the monomers is neither the only, nor the main, cause for the dimeric nature of the enzyme
dimer
-
2 * 28000, SDS-PAGE
dimer
-
2 * 27000, SDS-PAGE
dimer
-
2 * 28213, mass spectrometry, 2 * 30000, SDS-PAGE
dimer
-
2 * 26500, SDS-PAGE, both wild-type and mutant M80T
dimer
-
2 * 28108, mass spectrometry
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
-
active enzyme form
dimer
-
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
-
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
-
gel filtration and SDS-PAGE, crystal structure, overview
dimer
-
2 * 55663, electrospray mass spectrometry
dimer
-
structure comparisons, overview
dimer
Q8L1Z5
X-ray crystallography, only the TIM dimer is fully active
dimer
Q10657
X-ray crystallography, only the TIM dimer is fully active
dimer
-
X-ray crystallography, only the TIM dimer is fully active
dimer
P0A858
X-ray crystallography, only the TIM dimer is fully active
dimer
-
X-ray crystallography, only the TIM dimer is fully active
dimer
P00943
X-ray crystallography, only the TIM dimer is fully active
dimer
-
X-ray crystallography, only the TIM dimer is fully active
dimer
P50921
X-ray crystallography, only the TIM dimer is fully active
dimer
P66940
X-ray crystallography, only the TIM dimer is fully active
dimer
-
X-ray crystallography, only the TIM dimer is fully active
dimer
P62003
X-ray crystallography, only the TIM dimer is fully active
dimer
-
X-ray crystallography, only the TIM dimer is fully active
dimer
P36204
X-ray crystallography, only the TIM dimer is fully active
dimer
P04789
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
homodimer
A8B3A8, -
2 * 27000, SDS-PAGE; 2 * 27188, calculated from amino acid sequence
homodimer
-
2 * 26732, calculated from amino acid sequence
monomer
-
1 * 26879, equilibrium sedimentation
tetramer
-
4 * 24000, crystallographic data
tetramer
-
assembled as a dimer of dimers
tetramer
-
4 * 27000, SDS-PAGE
tetramer
-
X-ray diffraction data
monomer
-
1 * 27 831, electrospray mass spectrometry
additional information
-
reversible guanidinium hydrochloride induced equilibrium unfolding involves stable dimeric and monomeric intermediates
additional information
-
in solution the enzyme exhibits an equilibrium between inactive dimers and active tetramers
additional information
-
tetramer results from covalent attachment of two dimers that conserve similar association constants between their constituent monomers
additional information
-
in a yeast two-hybrid system, enzyme interacts with integrin alphaIIb cytoplasmic domain and binds weakly to its alphaV tail
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
-
structure determination and analysis of the monomeric enzyme, overview
additional information
-
structure analysis and loop interactions of TIM, overview
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
-
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
-
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 20-80C, 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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
TPI is a direct substrate of cyclin-dependent protein kinase 2, Cdk2, during etoposide-induced apoptosis, analysis by MALDI-TOF peptide finger printing. Phosphorylation of the recombinant TPI by recombinant cyclin A/Cdk2 kinase leading to reduced TPI activity, protection by olomoucine, a specific inhibitor of Cdk2
no glycoprotein
-
neither cytosolic nor chloroplastic enzyme is glycosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals are grown at 18C 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
-
crystal structure of the recombinant enzyme complexed with phosphoglycolohydroxamate, at 1.8 A resolution
-
simulation of both dimeric and monomeric (isolated from dimer) forms in explicit water at 27C and 1 bar. Significant cross-correlations between residue fluctuations are observed in the dimer, which result from the global counter-rotations of the two identical subunits in the essential modes of the dimer. The first essential mode contributing to 34% of overall motion of the dimer is strongly coupled to the loop 6's closure over the active site. The monomeric structure maintains relatively localized motions of the loops in the essential modes
-
hanging drop vapor diffusion method
-
triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution
-
determination of intrinsic fluorescence of wild-type and mutants lacking Trp residues, interpretation based on crystal structure. Fluorescence of all Trp residues is quenched by aromatic-aromatic interactions due to the proximity and orientation of the indole groups of Trp196 and Tro162. Quenching is also due to energy transfer to the charged resiudes that surround Trp75, Trp173, and Trp196
-
determination by molecular replacement, at 2.3 A resolution and in the closed state. Phosphate acts as a competitive inhibitor and occupies the binding pocket. Binding pocket has a very stable conformation even without a substrate
-
monomer, to 2.3 A resolution
-
high resolution structure of crystal form 2 employing the gel-tube method in microgravity
-
mutant E104D, at 1.85 A resolution. Mutant structure is similar to wild-type, mutant residue E104A is part of a conserved cluster of 10 residues, 5 from each subunit. This cluster forms a cavity that possesses an elaborate conserved network of buried water molecules that bridge the two subunits. In the E104D mutant, a disruption of contacts of the amino acid side chains in the conserved cluster leads to a perturbation of the water network in which the water-protein and water-water interactions that join the two monomers are significantly weakened and diminished
-
triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution
-
crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
-
mutant enzyme E65Q, hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
-
purified enzyme mutant E65Q in complex with reaction-intermediate analogue phosphoglycolohydroxamate, hanging drop method, TIM-PGH crystals are grown at room temperature, 0.004 ml of protein solution with 11 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl, 10 mM PGH, 1 mM DTT, 1 mM EDTA, and 1 mM NaN3, are mixed with 0.004 ml of well solution containing 0.1M acetate, pH 5.0, 24% PEG6000, 1 mM DTT, 1 mM EDTA, and 1 mM NaN3, X-ray diffraction structure determination and analysis at 0.82 A resolution
-
unliganded enzyme. Complete absence of electron density for the loop 6 residues. Disorder of this loop due to a missing slat bridge between residues at the N-and C-terminal ends of the loop
-
crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex, at 2.7 A resolution; hanging drop vapor diffusion method. Crystal structure of the enzyme-sulfate complex and the enzyme-2-phosphoglycolate complex at a 2.7 A resolution
-
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
-
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 -188C, whereas form B has unit-cell parameters A = 73.02, b = 79.8 and c = 172.85
-
crystal structure analysis
-
crystal structure analysis, overview
-
crystal structure of PfTIMat 2.2 A resolution or 2.8 A resolution, crystal structure of the enzyme in complex with phosphoglycolate at 1.9 A resolution, crystal structure of the enzyme in complex with glycerol phosphate at 2.4 A resolution, crystal structure of the enzyme in complex with 2-phosphoglycerate at 1.1 A resolution or 2.4 A resolution
-
E97Q and E97D mutant enzymes, hanging drop vapor diffusion method
-
enzyme in complex with 3-phosphoglycerate or glycerol 3-phosphate, hanging drop vapor diffusion method
-
mutant enzyme C126S in complex with PGA, hanging drop vapor diffusion method, using 20% (w/v) poly(ethylene glycol), 1 M HEPES buffer (pH 7.5), and 10 mM lithium sulfate, at 23C. Unliganded mutant enzymes C126S and C126A, hanging drop vapor diffusion method, using 24% (w/v) poly(ethylene glycol), 1 M HEPES buffer (pH 7.0), and 10 mM lithium sulfate
-
wild-type and mutant enzymes in complex with inhibitior 3-phosphoglycerate, 0.003 ml of 10 mg/ml protein in 100 mM triethanolamine-HCl, pH 7.6, are mixed with an equal volume of reservoir solution, the crystallization cocktail contains 0.1 M sodium acetate pH 4.0-5.5 and PEG 1450 varying from 8% to 24% in the reservoir, X-ray diffraction structure determination and analysis at 1.4-2.25 A resolutions
-
hanging drop vapor diffusion method, diffraction quality can only be obtained in the presence of inhibitors, monoclinic crystal form is obtained by cocrystallization with 20 mM 2-carboxyethylphosphonic acid with sodium acetate, pH 4.0, and 7% PEG 4000 as the precipitant buffer. An orthorhombic crystal form is obtained by cocrystallization with 20 mM 2-phosphoglycolic acid with 0.1 M sodium acetate, pH 4.2, and 5% PEG 4000 as the precipitant buffer. Hexagonal crystal forms are obtained under the same conditions with 2-phosphoglycolic acid, but their diffraction shows high disorder
-
hanging drop vapor diffusion method, using 0.1 M HEPES-Na, pH 7.5, and 1.4 M trisodium citrate dihydrate
A8B3A8, -
purified recombinant enzyme, 200 mg/ml protein with ligand in a ratio of 5:1 in 50 mM Tris-HCl, 50 mM NaCl, and 1 mM EDTA, pH 6.8, 4C, is mixed with 40% w/v PEG 4000 as precipitant, X-ray diffraction structure determination and analysis
-
purified recombinant enzyme by hanging drop vapour diffusion method, from 1.6 M trisodium citrate dihydrate, pH 6.5, X-ray diffraction structure determination and analysis at1.9 A resolution, modeling
-
purified recombinant C-terminally His6-tagged enzyme, sitting drop vapour diffusion method, room temperature, 0.003 ml of 18 mg/ml protein in 10 mM MES buffer, pH 6.5, and 15 mM NaCl, is mixed with 0.003 ml of reservoir solution containing 18% PEG MME 2000 as precipitant, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
structure of both a hexagonal and an orthorhombic crystal form to resolutions of 2.5 A and 2.3 A. In both crystal forms the enzyme exists as a tetramer of the (betaalpha)8-barrel. Hexagonal crystal form (crystallisation conditions 0.1 M HepesKOH (pH 7.5), 0.8 M sodium potassium phosphate) diffracts to 2.5 A and belongs to spacegroup P6(5)22/P6(1)22 with cell dimensions a = b = 186.9 A, c = 287.8 A, alpha = beta = 90, gamma = 120, suggesting two tetramers in the asymmetric unit. Orthorhombic crystals with cell dimensions a = 154.1 A, b = 91.0 A, c = 141.2 A, alpha = beta = gamma = 90 are obtained in 0.1 M sodium acetate (pH 4.6), 0.2 M ammonium sulfate, with PEG4000 at any concentration between 20% and 30% (w/v). Crystals grew within 48 hours at 20C
-
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method, crystal structure represents the most thermostable triosephosphate isomerase presently known in its 3D-structure
-
use of real time in situ atomic force microscopy to monitor the molecular processes that govern the crystallization of triosephosphate isomerase. Triosephosphate isomerase tetramers are the dominating growth units. The incorporation of growth units occurs through surface diffusion. Normal growth is dominated by the two-dimensional nucleation of triangular islands
-
monomeric enzyme variant with an engineered binding groove, m18bTIM, and the V233A mutant of this variant in complex with citrate, 2-phosphoglycolate, and glycerol 3-phosphate, to 1.89, 1.6, 2.3 and 2.0 A resolution, respectively
-
mutant A178L, unliganded and in complex with 2-phosphoglycolate, to 2.2 A and 1.89 A, respectively. Monomeric mutant mlA178L, unliganded and in complex with 2-phosphoglycolate, to 2.3 A and 1.18 A, respectively. Mutation A178L favors the closed conformation of the C-terminal hinge region
-
mutant enzyme R191S, hanging drop vapor diffusion method, crystal structure of the R191S mutant complexed with 2-phosphoglycolate is determined at 1.65 A resolution
P04789
mutant P168A, with and without 2-phosphoglycolate. Phosphate moiety of 2-phosphoglycolate is bound similarly as in wild-type, but interactions of the carboxylic acid moiety with the side chain of catalytic Glu167 differ
-
hanging drop vapor diffusion method, a crystal of the dimeric enzyme is soaked and diffracted in hexane and its structure solved at 2 A resolution. Its overall structure and the dimer interface are not altered by hexane
-
hanging drop vapour diffusion method, crystals of the enzyme in complex with one molecule of 3-(2-benzothiazolylthio)-1-propanesulfonic acid diffract to a resolution of 2 A. Unit cell dimensions: a = 42.87, b = 75.57, c = 146.45
-
purified recombinant monomeric enzyme by sitting drop method, 0.001 ml of protein solutioncontaining 25 mg/ml protein in 20 mM Tris-HCl , pH 7.4, and 1.0 mM EDTA is mixed with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 7.5, 10% PEG 6000, and 5% MPD, X-ray diffraction structure determination and analysis
-
comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms
-
genetically engineered enzyme variant, at 2.6 A resolution
-
resolution of 2.1 A in a new crystal form grown at pH 8.8 from PEG6000
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
from 25 to 95C, profound unfolding and loss of 50% activity occurs at pH 3.0, also when the enzyme is directly placed at 95C during 150 s. TIM has similar secondary structure but different surface features at pH 3.0, and shows increased susceptibility to thermal unfolding at pH 3.0
6
7
-
37C, 6 h, stable. Irreversible conformational changes below and above
6.5
8.5
-
20 h, stable
7
-
-
22C, stable indefinitely
7
-
-
25-95C with slow elevation of temperature, no loss of activity, also no loss when the enzyme is directly placed at 95C during 150 s
8.1
-
-
22C, stable indefinitely
10
-
-
25-95C with slow elevation of temperature, limited loss of activity, also no loss when the enzyme is directly placed at 95C during 150 s
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
-
-
half-life of wild-type enzyme: 58 min
22
-
-
pH 7, stable indefinitely
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 95C induces cold denaturation in partially denatured TIM
25
-
-
half-life of wild-type enzyme: 10 min, half-life of mutant enzyme A238S: 27 min; mutant A238S, half-life: 27 min; wild-type enzyme, half-life: 10 min
37
-
-
half-life of mutant enzyme H12N/K13G is 11.5 min
40
-
-
5 min, cytosolic enzyme, about 50% of activity
42
-
-
stable for at least 30 min
42
-
P04789
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
48
-
-
the melting temperature of the active form P1 of TIM is 48C
50
-
-
50 min, no loss of activity
50
-
-
10 min, complete loss of activity
50
-
-
stable up to
51
-
-
half-life of mutant enzyme H13G is 11.5 min
55
-
-
5 min, chloroplastic enzyme, about 30% loss of activity
60
-
-
pH 8.1, half-life: 4 h
60
-
-
30 min, complete inactivation
60
-
-
the melting temperature of the wild type enzyme is at 60C
63
-
-
if denaturation is carried out at temperatures above 64.0C, a partially folded species is formed in a time short enough to avoid the occurence of deleterious aggregation reactions
64
-
-
half-life of mutant enzyme H12N is 11.5 min
64
-
-
the melting temperature of the active form P2 of TIM is 64C
68
-
-
half-life of wild-type recombinant enzyme is 11.5 min
94
-
-
half-life of wild-type recombinant enzyme is 11.5 min
96
-
-
half-life of mutant enzyme H12N/K13G is 11.5 min
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
-
-
Lys13 plays a crucial role in the functional adaptation of the thermophilic enzyme to high temperatures
additional information
-
-
crystal structure represents the most thermostable triosephosphate isomerase presently known in its 3D-structure
additional information
-
-
Thermal melting of PfuTIM in buffers of different pH, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at a concentration of 2 ng/ml or 0.4 ng/ml stable for 24 h
-
bovine serum albunin assists in the refolding and regain of TIM enzyme activity by providing framework for structure formation
-, Q0ZAG6
destabilization of TIM by SDS at pH 3.0
-
global unfolding effected by heat and denaturants such as urea or guanidine hydrochloride is irreversible
-
native form of enzyme is stable to unfolding by SDS
-
stable to photooxidation with rose bengal
-
no loss of activity when dialyzed extensively against 0.1 M Tris/HCl, pH 7.6, containing 1 mM dithiothreitol, 1 mM EDTA, 1 mM sodium azide and 0.2 M ammonium sulfate
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
guanidine-HCl
-
6 M, incubation times longer thah 10 min lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme
guanidine-HCl
-
2.4 M, the unfolding transition is complete
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
guanidine-HCl
P04789
3.2 M, half-life of wild-type enzyme: 30 min, half-life of mutant enzyme D227N: 20 min, half-life of mutant enzyme D227A: 15 min, half-life of mutant enzyme R191S: 8 min, half-life of mutant enzyme R191A: 19 min
urea
-
8 M, incubation times longer than 5 h lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme
urea
-
the unfolding transition midpoit is 3.5 M for Y74Cox and 5.5 M for the wild-type enzyme. The dimeric wild-type enzyme retains considerable secondary, tertiary, and quarternary structure even in 8 M urea. Urea unfolding profiles of Y74Cox in urea solution obtained by fluorescence and circular dichroism approximate a two-state transition and do not show the presence of stable intermediates over a wide range of denaturant concentrations. In wild-type enzyme the unfolding results in gradual change in spectroscopic properties
urea
-
the enzyme is denatured in buffer with 3 M urea
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, pH 7.0, 2.5 mM ammonium sulfate, 1 mM EDTA, stable for at least 2 years
-
4C, purified recombinant enzyme, 40 days, no loss of activity
A8B3A8, -
0-4C, pH 6.5, 2.5 mM ammonium sulfate, stable for at least 2 years
-
stable upon prolonged storage in 0.1 M Tris/HCl buffer, pH 7.6, containing 1 mM dithiothreitol, 1 mM EDTA, 1 mM sodium azide and 0.2 M ammonium sulfate
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3 isoenzymes
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography
-
recombinant wild-type enzyme from TIM-deficient Escherichia coli strain DF502 by anion exchange chromatography
-
wild-type and mutant enzymes H12N, H13G and H12N/K13G
-
recombinant enzyme
-
3 distinct electrophoretic forms: I, II, III
-
3 isoenzymes
-
Ni-NTA agarose column chromatography
-
recombinant mutant E104D
-
Ni-NTA column chromatography
-, Q0ZAG6
native enzyme from shoots in a chromatographic process
-
wild-type and mutant enzyme A238S
-
recombinant enzyme
-
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephacryl-200 gel filtration
-
recombinant wild-type and mutant enzymes from TIM-deficient Escherichia coli strain AA200 by gel filtration and ion-exchange chromatography
-
wild-type and mutant enzyme Y74C
-
wild-type enzyme and mutant enzymes Y74C and Y74G
-
recombinant enzyme
-
ammonium sulfate precipitation and Mono-Q column column chromatography
A8B3A8, -
DEAE-Sepharose column chromatography
-
recombinant TIM from Escherichia coli
-
native enzyme 2400fold from cell surface by hydrophobic interaction and anion exchange chromatography, followed by adsorption chromatography
-
recombinant enzyme from Escherichia coli strain M15 to homogeneity by nickel affinity chromatography and gel filtration
-
recombinant C-terminally His6-tagged TIM from Escherichia coli by metal affinity chromatography
-
wild-type and mutant enzyme H12N/K13G
-
wild-type enzyme and mutant enzymes C14A, C14P, C14S, C14T, C14V and C14G. Attempts to purify mutant enzymes C14M and C14L are unsuccessful, the enzymes exhibit a strong tendency to undergo aggregation
-
ammonium sulfate precipitation and CM-Sepharose column chromatography
Trypanosoma brucei subsp. brucei
-
recombinant monomeric enzyme from Escherichia coli strain BL21 (DE3)
-
genetically engineered enzyme variant
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-, P35144
expression as wild-type enzyme and fusion protein with an N-terminal tail of six histidine residues
-
expression of the wild-type enzyme in TIM-deficient Escherichia coli strain DF502
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli TOP10
-
expressed in Escherichia coli BL21(DE3) or BL21-CodonPlus(DE3)RIL cells. The preparations of native TIM contain two isolatable stable catalytically active forms P1 and P2 of TIM
-
expression of TPI in Spodoptera frugiperda Sf21 cells using the baculovirus transfection system
-
in expression vector pET-23(a) with C-terminal His6 tag fused in frame, expressed in Escherichia coli BL21(DE3) cells
-, Q0ZAG6
overexpression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli AA200 cells
-
expressed in Escherichia coli AA200 cells (a null mutant of inherent TIM gene)
-
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in TIM-deficient Escherichia coli strain AA200
-
mutant enzymes E97Q and E97D are expressed in Escherichia coli AA200 cells
-
clone identified in screen for arsenate resistance
-, Q0H294
expression of the N-terminally His6-tagged enzyme in Escherichia coli strain M15
-
overexpression in Escherichia coli in fusion with glutathione S-transferase. The GST-PfuTIM fusion product partitions mainly into the insoluble fraction of the whole cell lysate
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)pLysS cells
A8B3A8, -
expressen in Escherichia coli
-
expression of TIM in Escherichia coli
-
expression of wild-type enzyme and mutant enzymes C126S and C126A in Escherichia coli
-
mutant enzyme K12G is expressed in Escherichia coli strain DF502
-
expression in Escherichia coli
-
overexpression of the enzyme in Escherichia coli strain M15
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of C-terminally His6-tagged TIM in Escherichia coli cytoplasm in a natively folded, enzymatically active form
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21 pLys S cells
Trypanosoma brucei subsp. brucei
-
expression of the monomeric enzyme in Escherichia coli strain BL21 (DE3)
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme expression is upregulated in lung squamous cell carcinoma
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K174G/T175G/A176G
-
16.5fold decrease in turnover number for D-glyceraldehyde 3-phosphate, 7.9fold increase in Km-value for D-glyceraldehyde 3-phosphate, 8fold decrease in turnover number for dihydroxyacetone phosphate, 2.6fold increase in Ki-value for arsenate, 10.4fold increase in Ki-value for 2-phosphoglycolate
V167G/W168G
-
17.9fold decrease in turnover number for D-glyceraldehyde 3-phosphate, 2.6fold increase in Km-value for D-glyceraldehyde 3-phosphate, 8.6fold decrease in turnover number for dihydroxyacetone phosphate, 2.7fold increase in Ki-value for arsenate, 8.1fold increase in Ki-value for 2-phosphoglycolate
V167G/W168G/K174G/T175G/A176G
-
2529fold decrease in turnover number for D-glyceraldehyde 3-phosphate, 8.5fold increase in Km-value for D-glyceraldehyde 3-phosphate, 1720fold decrease in turnover number for dihydroxyacetone phosphate, 2.8fold increase in Ki-value for arsenate, 12.4fold increase in Ki-value for 2-phosphoglycolate
Y208T/G210A/S211G
-
site-directed mutagenesis
H12N
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 64C compared to 68C for the wild-type enzyme
H12N/K13G
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 37C compared to 68C for the wild-type enzyme
H13G
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 51C compared to 68C for the wild-type enzyme
F12W
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W162F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W162F/W173F/W196F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W173F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W196F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W75F
-
mutant constructed for fluorescence quenching studies, catalytic properties similar to wild-type
W75F/W162F/W173F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W75F/W162F/W196F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
W75F/W173F/W196F
-
mutant constructed for fluorescence studies, catalytic properties similar to wild-type
D213A
-
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
D213A
-
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
D213Q
-
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
D213Q
-
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
K183A
-
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
K183A
-
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
K183S
-
Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type
K183S
-
disruption of the salt bridge between residues D213 and K183, kinetic parameters similar to wild-type
E104D
-
mutation involved in human triosephosphate isomerase defiecency autosomal disease. Mutant exhibits normal catalytic activity but shows impairments in the formation of active dimers and low thermostability. E104A is part of a conserved cluster of 10 residues, 5 from each subunit. This cluster forms a cavity that possesses an elaborate conserved network of buried water molecules that bridge the two subunits. In the E104D mutant, a disruption of contacts of the amino acid side chains in the conserved cluster leads to a perturbation of the water network in which the water-protein and water-water interactions that join the two monomers are significantly weakened and diminished
E104D
-
in patients homozygous for this mutation, only 2-20% of TIM catalytic activity is left
E65Q
-
the variant of Leishmania mexicana TIM has a much enhanced stability but its catalytic properties are the same as wild-type leishmanial TIM
C126A
-
the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme
C126M
-
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme
C126S
-
the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme
C126T
-
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme
C126V
-
the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme
C13D
-
the mutant displays significant reduction in catalytic activity when compared with wild type enzyme (about 7.4fold decrease in kcat). The C13D mutant dissociates at concentrations above 1.25 mM
C13E
-
the mutant displays significant reduction in catalytic activity when compared with wild type enzyme (about 3.3fold decrease in kcat). The C13E mutant retains dimeric at concentrations above 1.25 mM
E165A
-
the mutant shows an approximately 9000fold drop in activity
E97D
-
the mutant shows a 100fold reduction in kca
E97Q
-
the mutant shows a 4000fold reduction in kca
F96H
-
site-directed mutagenesis, the mutant exhibits highly reduced catalytic efficiency and decreased substrate-binding affinity, as well as reduced sensitivity to inhibitor 3-phosphoglycerate, compared to the wild-type enzyme
F96S
-
site-directed mutagenesis, the mutant exhibits highly reduced catalytic efficiency and decreased substrate-binding affinity, as well as reduced sensitivity to inhibitor 3-phosphoglycerate, compared to the wild-type enzyme
W11F/W168F/Y74W
-
site-directed mutagenesis, template is the available crystal structure of the enzyme from Giardia lamblia, which contains a Trp residue at position 47. The mutant dissociates at low protein concentrations, and exhibits considerably reduced stability in the presence of denaturants, urea and guanidinium chloride, and it shows approximately 20fold reduction in kcat at low protein concetrations compared to the wild-type enzyme, but the mutant mutant shows an enhancement of activity of 21.9fold at higher concentration range
Y74C
-
urea unfolding profiles of Y74Cox in urea solution obtained by fluorescence and circular dichroism approximate a two-state transition and do not show the presence of stable intermediates over a wide range of denaturant concentrations. In wild-type enzyme the unfolding results in gradual change in spectroscopic properties. The unfolding transition midpoit is 3.5 M for Y74Cox and 5.5 M for the wild-type enzyme
Y74C
-
inhibitory effect of KFGNGSYTGEVS and KYGNGSCTGEVS is more pronounced compared to the wild-type enzym. Mutant enzyme has reduced stability due to an interface cavity
R111T/R112A/E114K/E115G
-
site-directed mutagenesis, destroying of four ion pair interactions by replacing four of the charged residues in helix 4 with structurally analogous residues from the psychrophile Methanococcoides burtonii TIM to create a mutant, mPfuTIM, that is less kinetically stable than wild-type PfuTIM
C126A
-
turnover number for D-glyceraldehyde 3-phosphate is 1.5fold lower than the wild-type value, KM-value for D-glyceraldehyde 3-phosphate is 1.4fold lower than the wild-type value, turnover number for dihydroxyacetone phosphate is 4.3fold lower than the wild-type value, KM-value for dihydroxyacetone phosphate is 3.7fold lower than the wild-type value
C126S
-
mutant enzyme shows greater susceptibility to thermal denaturation than wild-type enzyme, turnover number for dihydroxyacetone phosphate is 8.3fold lower than the wild-type value, KM-value for dihydroxyacetone phosphate is 3.5fold lower than the wild-type value
D225Q
-
mutation causes minor drops in Km and kcat value without changes catalytic efficiency. Temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain
K12G
-
the mutation results in a ca. 50fold increase in Km for the substrate glyceraldehyde 3-phosphate (GAP) and a 60fold increase in Ki for competitive inhibition by 2-phosphoglycolate, a 12000fold decrease in kcat for isomerization of GAP, and a 6000000fold decrease in kcat/Km for GAP
K17A/Y46A/D48F/Q82A/D85S
-
mutation of residues in the dimer interface of enzyme
K17L/Y46F/D48F/Q82F/D85L
-
mutation of residues in the dimer interface of enzyme. Decrease in catalytic efficiency by 4 orders of magnitude
K17L/Y46F/D48Y/Q82A/D85A
-
mutation of residues in the dimer interface of enzyme. Decrease in catalytic efficiency by 4 orders of magnitude
H12N/K13G
-
mutant enzyme shows increases thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 96C compared to 94C of the wild-type enzyme
A178L
-
decrease in catalytic efficiency. Crystallization data reveal a more disordered loop-6 in the structure of unliganded A178L. Liganded structures show minimal differences to wild-type
C14A
-
the KM-value for D-glyceraldehyde 3-phosphate is 1.2fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is 90% of the value for the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 1.2fold higher than the value for the wild-type enzyme. The turnover-number for glycerone phosphate is comparable to the value for the wild-type enzyme
C14F
-
the Ki-value for 3-phosphoglycolate is nearly 3times higher than the Ki-value for the wild-type enzyme. The ratio of elimination to isomerization reactions is higher than in the wild-type enzyme. The KM-value for D-glyceraldehyde 3-phosphate is 10.2fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is 2.7fold higher than the value for the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 2280fold lower than the value for the wild-type enzyme. The turnover-number for glycerone phosphate is 3000fold lower than the value for the wild-type enzyme
C14L
-
Cys14Leu mutant has the tendency to aggregate, reduced stability and altered kinetics
C14P
-
the KM-value for D-glyceraldehyde 3-phosphate is 94% of the value for the wild-type enzyme. The KM-value for glycerone phosphate is 58% of the value for the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 85% of the value for the wild-type enzyme. The turnover-number for glycerone phosphate is 81% of the value for the wild-type enzyme
C14S
-
the KM-value for D-glyceraldehyde 3-phosphate is 1.4fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is identical to the value of the wild-type value. The turnover number for D-glyceraldehyde 3-phosphate is 1.15fold higher than the value for the wild-type enzyme. The turnover-number for glycerone phosphate is nearly identical to the value of the wild-type enzyme
C14S
-
wild-type-like enzyme that is resistant to the action of sulfhydryl reagents methylmethane thiosulfonate and 5,5-dithiobis(2-nitrobenzoate)
C14S/A69C
-
similar in kinetic parameters to wild-type TbTIM and the single mutant C14S. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14S/A73C
-
greatly reduced kcat value. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14S/S71C
-
similar in kinetic parameters to wild-type TbTIM and the single mutant C14S. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14S/S79C
-
similar in kinetic parameters to wild-type TbTIM and the single mutant C14S. Mutant binds 50 times more 1-anilino-8-naphthalene sulfonate than wild-type and is susceptible to digestion with subtilisin
C14T
-
the KM-value for D-glyceraldehyde 3-phosphate is 1.2fold higher than the value for the wild-type enzyme. The KM-value for glycerone phosphate is 79% of the value of the wild-type enzyme. The turnover number for D-glyceraldehyde 3-phosphate is 92% of the value for the wild-type enzyme. The turnover-number for glycerone phosphate is 92% of the value of the wild-type enzyme
D227A
P04789
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 2.2fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 5fold lower than the value for the wild-type enzyme
D227N
P04789
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 3.75fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 3.5fold lower than the value for the wild-type enzyme
E168D
-
catalytically inert. Dimer formation with Trypanosoma cruzi dimer interface mutant C15Acauses a drop in activity by 50%
P168A
-
mutation beside catalytic residue Glu167. Mutant turnover number is 50fold reduced, Km value is 2fold reduced
R191A
P04789
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 10.4fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 10.6fold lower than the value for the wild-type enzyme
additional information
-, P48491
construction of a T-DNA insertion mutant that shows a fivefold reduction in transcript, reduced TPI activity, and a severely stunted and chlorotic seedling that accumulates dihydroxyacetone phosphate, glycerol, and glycerol-3-phosphate. Methylglyoxal, a by-product of dihydroxyacetone phosphate, also accumulated in the pdtpi mutant. Lipid profiling reveals lower monogalactosyl but higher digalactosyl lipids in the mutant compared to the wild-type, phenotype, overview. Exogenous glycolytic intermediates do not rescue the pdtpi phenotype. Metabolic pathways affected by a mutation in pdTPI during postgerminative seedling transition from heterotrophic to photoautotrophic development, overview
M80T
-
analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis
additional information
-
mutation wasted away is a recessive, hypomorphic mutation that causes progressive motor impairment, vacuolar neuropthology, and severely reduced lifespan. Mutation affects the gene for triosephosphate isomerase. There is no genetic evidence that the mutation leads to misfolded or aberrant protein. Mutation may lead to an accumulation of methylglyoxal and the consequent enhanced production of advanced glycation end products
I170V
-
the mutation is asociated with a mild form of TIM deficiency
additional information
-, Q7X216
overexpression of isoform Tpi2 in a Tpi1-deficient mutant restores the growth deficiency on minimal medium containing glucose or glycerol; Tpi1-deficient mutant grows weakly on minimal medium containing glucose or glycerol, but grows normally on gluconate. Residual enzymic activity on glucose or glycerol is due to presence of enzyme isoform Tpi2
additional information
-
modulation of gene expression around wild-type level by replacing the native promoter with libraries of synthetic promoters. Enzyme is present in high excess in wild-type cells. 10% residual activity still support more than 70% of the wild-type glycolytic flux. At at residual triosephosphate isomerase activity of 3%, dihydroxyacetone phosphate level increases four times and coincides with an increase in formate production
A238S
-
catalytic efficiency of the mutant enzyme is somewhat reduced, and its stability is considerably increased. The half-life at 25C is 27 min compared to 10 min for the wild-type enzyme; mutant enzyme A238S has a higher thermal stability than the wild-type enzyme. The turnover number of the mutant enzyme is somewhat lower than that observed for the wild-type enzyme, the Km-value for D-glyceraldehyde 2-phosphate is somewhat higher
additional information
-
some TPIs are found on the paired helical filaments in Tau transgenic mice
F96W
-
site-directed mutagenesis, the mutant exhibits reduced catalytic efficiency and decreased substrate-binding affinity, as well as reduced sensitivity to inhibitor 3-phosphoglycerate, compared to the wild-type enzyme. The wild-type enzyme shows a loop-open state for 3-phosphoglycerate binding at the active site, while the mutant F96W shows both open and closed states
additional information
-
decrease in ligand affinity in F96 mutants can be a consequence of differences in the water network connecting residue 96 to Ser73 in the vicinity of the active site
Y74G
-
site-directed mutagenesis, the mutation Tyr74Gly significantly reduces the stability of the dimer, mutation-induced alteration in the backbone conformation of Lys12, structure comparison to the wild-type enzyme
additional information
-, Q0H294
expression of enzyme confers arsenic tolerance to Escherichia coli XL1 Blue and DF502
K17P/Y46A/D48L/Q82T/D85A
-
mutation of residues in the dimer interface of enzyme
additional information
-
mutation of five residues in the dimer interface of enzyme. Obtained proteins are soluble, dimeric, and compact. Proteins obtained from direct evolution experiments show wild-type-like catalytic activity, while their stability is decreased. In silico-designed proteins are very stable dimers that bind substrate with a wild-type-like Km value, albeit they exhibit a very low kcat
H47N
-
mutant His47Asn, dimer is considerably less stable than wild-type trypanosomal enzyme
additional information
-
wild-type enzyme consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit. By replacing 15 residues of the major interface loop by another 8-residue fragment, a variant is constructed that is a stable and monomeric protein with TIM activity, monoTIM. The turnover numer of the monomeric form is 100fold lower
additional information
-
hybrids of Trypanosoma cruzi enzyme carrying residues of the dimer interface from Trypanomsoma brucei and vice versa, and hybrids with one monomer in the enzyme dimer from Trypanosoma cruzi, and the second monomer from Trypanosoma brucei. Solvent exposure of the interfacial C15 depends predominantly on the characteristics of the adjoining monomer. Half of the activity of each monomer depends on the integrity of each of the two C15-loop3 portions of the interface
additional information
-
introduction of mutation V233A into a monomeric enzyme variant with an engineered binding groove, m18bTIM. Mutation V233A restores the structural properties of loop-7, the binding site of a conserved water molecule between loop-7 and loop-8 and the binding site of the phosphate moiety of wild-type in the m18bTIM background. The active site of the V233A mutant can bind transition state analogs and suicide inhibitors competently, the catalytic efficiency of the V233A mutant is too low to be detected
additional information
-
a reporter protein fused to a Saccharomyces cerevisiae peptide containing the sequence corresponding to the 22-residue fragment, including residues K155, D158, W159, A160 and K161, of the Trypanosoma brucei TPI enzyme, is not targeted to glycosomes
R191S
P04789
mutant enzyme with reduced stability to 3.2 M guanidinium-HCl and reduced thermal stability at 42C. The ratio of turnover number to Km for D-glyceraldehyde 3-phosphate as substrate is 2fold lower than the value for the wild-type enzyme. The ratio of turnover number to Km for glycerone phosphate as substrate is 6.7fold lower than the value for the wild-type enzyme
additional information
Trypanosoma brucei subsp. brucei
-
the monomeric form of TIM does not catalyze any reactions of D-glyceraldehyde 3-phosphate at the enzyme active site, either in the absence or in the presence of phosphite dianion
C15A
-
dimer formation of mutant protein with intact Trypanosoma brucei monomer, maximal inhibition of catalysis by mutation is 60%. Dimer formation with catalytically inert Trypanosoma brucei mutant E168D causes a drop in activity by 50%
additional information
-
hybrids of Trypanosoma cruzi enzyme carrying residues of the dimer interface from Trypanomsoma brucei and vice versa, and hybrids with one monomer in the enzyme dimer from Trypanosoma cruzi, and the second monomer from Trypanosoma brucei. Solvent exposure of the interfacial C15 depends predominantly on the characteristics of the adjoining monomer. Half of the activity of each monomer depends on the integrity of each of the two C15-loop3 portions of the interface
additional information
-
construction of a monomeric enzyme form with loop-1 one residue shorter than monoTIM, which is constructed by replacing 15 residues of the major interface loop by another 8-residue fragment. The catalytic activity and stability of the new seven-residue Loop-1 enzyme variant is similar with that of monoTIM
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
unfolding of triosephosphate isomerase in urea is highly cooperative, and no folding intermediate is detected. The thermodynamic parameters just reflect the unfolding of dissociated folded monomer to fully unfolded monomer transition. Unfolding follows an irreversible two-state step with a slow aggregation process. The two subunits of the active enzyme unfold independently
-
renaturation into catalytic active enzyme by removal of the dissociating agent
-
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
-
inhibitor 2-phosphoglycolate brings about a large decrease in the unfolding rate constant of the protein. Thermodynamics of binding reveal a dimeric transition state
-
reversible denaturation and renaturation of the homodimeric enzyme induced by urea and guanidine-HClm renaturation is fully reversible. Unfolding experiments do not reach an equilibrium, owing to a very slow dissociation and/or unfolding process. By contrast, equilibrium is reached in the refolding direction
-
study on the effect of viscosity in the unfolding and refolding of enzyme. Two transitions indicate a three-state model with a monomeric intermediate. The bimolecular association producing the native dimer is limited by diffusional events of the polypeptide chains through the solvent
-
study on unfolding and refolding of enzyme in guanidinium hydrochloride and comparison with enzyme from Entamoeba histolytica. 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
-
temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain
-
the refolding reaction of the thermally denatured enzyme obeys second-order kinetics and leads to the formation of dimer nativelike enzyme, dimerization is coupled to the regain of a large amount of secondary structure
-
protein unfolded in 3.2 M guanidinium-HCl is diluted to final concentrations of 0.32 M guanidinium-HCl, 16% recovery of wild-type enzyme after 72 h, 2.1-2.6% recovery of the mutant enzymes D227N, D227A, R191S and R191A after 72 h
P04789
unfolding/refolding reactions of monomeric enzyme evaluated using the two-state model
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
Clostridium difficile
-
specific polymerase chain reaction protocols used to determine the prevalence of toxigenic Clostridium difficile in Vhembe, South Africa. The study confirms the usefulness of PCR methodologies in the detection of toxigenic Clostridium difficile and suggests that Clostridium difficile is responsible for a small, but underappreciated, proportion of diarrheal cases in the region
medicine
Clostridium difficile
-
specific polymerase chain reaction protocols used to determine the prevalence of toxigenic Clostridium difficile in Vhembe, South Africa. The study confirms the usefulness of PCR methodologies in the detection of toxigenic Clostridium difficile and suggests that Clostridium difficile is responsible for a small, but underappreciated, proportion of diarrheal cases in the region
medicine
-
analysis of key aspects of triosephosphate isomerase deficiency glycolytic enzymopathy pathogenesis identified using the TPIsugarkill mutation M80T, a Drosophila model of the human disease deficiency. Mutant protein is expressed, capable of forming a homodimer, and is functional. However, the mutant protein is degraded by the 20S proteasome core leading to loss-of-function pathogenesis
diagnostics
-
triosephosphate isomerase is a serum marker for human lung squamous cell carcinoma
medicine
-
in drug-resistant SGC7901 cells induced by vincristine sulfate, triosephosphate isomerase is downregulated.The sensitivity of TPI-SGC7901/VCR cells to adriamycin, vincristine, 5-fluorouracil and cis-dichlorodiamine platinum, as well as the accumulation and retention to adriamycin, are significantly increased when compared to their control cell lines
medicine
-
67% of 39 patients suffering from adverse reactions to lychee show allergic reactions resp. IgE binding of their sera to enzyme protein
medicine
-
triosephosphate isomerase is a promising antischistosome vaccine antigen
medicine
-
evaluation of the ability of naive monocyte-derived dendritic cells to sensitize peripheral blood mononuclear cells to the Schistosoma vaccine candidate MAP4 using a priming in vitro assay. MAP4 is a multiple antigen peptide containing B- and T-cell epitopes derived from the enzyme triose phosphate isomerase. Cytokine production from activated MAP4 priming in vitro cells is predominantly Th1-like, consisting mainly of IFN-gamma. Naive donor dendritic cells, sensitized with MAP4, thus are able to prime and clonally expand MAP4-specific T cells towards a Th1-type response
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
additional information
-
the glycolytic enzyme triosephosphate isomerase occupies a central position in the development of structural and mechanistic enzymology