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Enzyme Nomenclature
Information on EC 5.3.1.1 - triose-phosphate isomerase
for references in articles please use BRENDA:EC5.3.1.1
Word Map on EC 5.3.1.1
- 5.3.1.1
-
aldolase
- giardia
- dihydroxyacetone
-
assemblage
- duodenalis
- enolase
- phosphoglycerate
-
barrel
-
zoonotic
- trypanosoma
- dhap
- chicken
- fructose
-
fecal
- giardiasis
- brucei
-
isomerases
-
multilocus
- gapdh
- malate
- cysts
-
phosphofructokinase
- cryptosporidium
- cruzi
- hexokinase
-
hemolytic
-
enediolate
-
stool
- parvum
- schistosoma
-
deamidation
- fructose-1,6-bisphosphate
- methylglyoxal
- 2-phosphoglycolate
- lamblia
- glycerol-3-phosphate
-
phosphoglucose
-
alpha-enolase
-
fructose-bisphosphate
-
dianion
- 1,6-bisphosphate
- glycosomes
- transaldolase
-
glucosephosphate
-
hungarian
-
subgenotype
-
enzymopathy
- phosphite
-
tim-barrel
- hominis
- synthesis
- medicine
- diagnostics
- analysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
5.3.1.1
-
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RECOMMENDED NAME
GeneOntology No.
triose-phosphate isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Glyceraldehyde 3-phosphate = glycerone phosphate
upon binding of ligand, the side chain of Glu167 flips from the inactive swung-out to the active swung-in conformation. A concerted movement of loop 6 and loop 7 from unliganded-open to liganded-closed is facilitated by the interactions of the phosphate moiety with loop 7. Rotation of the Gly211-Gly212 peptide plane of 90° is involved in this concerted movement
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
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
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
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
reaction mechanism via enediolate intermediate through proton abstraction by the catalytic base Glu167, overview
-
D-Glyceraldehyde 3-phosphate = glycerone phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
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CAS REGISTRY NUMBER
COMMENTARY
9023-78-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
-
multiple forms of triosephosphate isomerase are the consequence of minor post-synthetic alteration(s) of form A, three major forms: A, B, C
-
-
-
-
-
-
UniProt
-
-
-
bifunctional enzyme, phosphoglycerate kinase/triosephosphate isomerase
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
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
physiological function
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 chloroplastic isoform participates in the Calvin-Benson cycle
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
the plastid isoform of triose phosphate isomerase plays a crucial role in this transition from heterotrophic to autotrophic growth
physiological function
-
the enzyme is involved in glycogen catabolism
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
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
isomerization of D-glyceraldehyde 3-phosphate in D2O proceeds with 49% intramolecular transfer of the 1 H label from substrate to product dihydroxyacetone phosphate
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
the active site of free enzyme, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
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
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
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
-
the reaction is essential in vivo
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
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
-
TIM is highly specific for the substrates
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
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
-
key reaction in glycolysis
-
?
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
?
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
r
glycolaldehyde
?
-
TIM-catalyzed reactions of glycolaldehyde are activated by phosphite dianion, kinetics, overview
-
-
?
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
-
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
-
-
-
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
?
-
-
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
?
-
enzyme is involved in arsenate reduction
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
Q5CSE7
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
-
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
the reaction is essential in vivo
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
-
key reaction in glycolysis
-
?
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
Q5CSE7
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
Q6GIL6
-
-
-
r
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
-
-
-
-
r
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
-
additional information
?
-
Q0H294
enzyme is involved in arsenate reduction
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
2,6-dibenzyl-4-[(5-nitrothiophen-2-yl)methylidene]-1,2,6-thiadiazinane-3,5-dione 1,1-dioxide
-
irreversible inhibitor
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
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
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
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
cyclo[Trp-Tyr(OSO3Na)-D-Phe-Thr(OSO3Na)-Lys(benzyloxycarbonyl)-]
-
noncompetitive, reversible
ethyl 3-(3,5-di-tert-butyl-4-hydroxyphenyl)-1,2,4-thiadiazole-5-carboxylate
-
-
GSSG
-
oxidized glutathione is a strong inhibitor of the enzyme at low concentrations
H2O2
the inhibition of the enzyme is negligible when incubated with 0.1 mM H2O2, whereas a 10% inhibition is observed with 1 mM H2O2
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
methylbrevifolin carboxylate
-
molecular docking simulations and enzyme binding structure, and inhibition kinetics, overview
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
2,2'-methylenebis(1,3-benzothiazole)
-
40% inactivation at 0.05 mM, irreversible
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
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
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)
about 50% inhibition at about 0.05 mM
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
-
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
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
-
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
about 50% inhibition at about 0.05 mM
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
-
the sensitivity of enzyme from Trypanosoma cruzi is about 40times higher than that of Trypanosoma brucei and 200times higher than that of Leishmania mexicana
methylmethane thiosulfonate
-
0.6 mM, 2 h, complete loss of activity, dissociates the dimeric enzyme inducing formation of a compact monomeric state
methylmethane thiosulfonate
-
induces 75% enzyme inactivation within 15 min at 0.25 mM concentration
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
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
Phosphoglycolohydroxamate
-
the reaction-intermediate analogue binds to the active site with two hydrogen-bonding interactions between PGH and the Glu167 side-chain oxygen atoms
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
-
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
-
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
-
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
-
stronger inhibition by alpha-(1,3)-mannooligosaccharides than with triose, binding constants, overview
-
additional information
-
brevifolin carboxylate derivatives isolated from Geranium bellum selectively inactivate the enzyme partially, no inhibition by methyl tri-O-methylbrevifolin carboxylate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.091
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.14
D-glyceraldehyde 3-phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
0.25
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
0.25
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.25
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
0.27
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.28
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C
0.28
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C
0.29
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.3
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126S
0.31
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C
0.31
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C
0.31
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
0.35
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25°C
0.35
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
0.35
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
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
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
0.45
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
0.47
D-glyceraldehyde 3-phosphate
in 100 mM triethanolamine, pH 7.4, at 25°C
0.5
D-glyceraldehyde 3-phosphate
-
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C
0.62
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
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, 25°C
0.69
D-glyceraldehyde 3-phosphate
-
mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C
0.69
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C
0.8
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126A
0.87
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, tetrameric enzyme form
0.97
D-glyceraldehyde 3-phosphate
-
presence of methyl methanethiosulfonate
1
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.09
D-glyceraldehyde 3-phosphate
-
mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C
1.1
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
1.2
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C
1.2
D-glyceraldehyde 3-phosphate
-
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C
1.2
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.26
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C
1.4
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1.5
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C; mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
2.44
D-glyceraldehyde 3-phosphate
-
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C
3.04
D-glyceraldehyde 3-phosphate
in 100 mM triethanolamine (pH 7.4), at 25°C
3.7
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme K174G/T175G/A176G
4
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
8.6
D-glyceraldehyde 3-phosphate
-
presence of 2-carboxyethyl methanethiosulfonate
50
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
0.0025
dihydroxyacetone phosphate
-
in 100 mM Tris pH 7.8, at 25°C
0.077
dihydroxyacetone phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
0.49
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.59
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.7
dihydroxyacetone phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
0.7
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.7
dihydroxyacetone phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
4
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
18
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
0.69
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C
1
D-glyceraldehyde 3-phosphate
-
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C
1.04
D-glyceraldehyde 3-phosphate
-
mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C
1.7
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
4.2
D-glyceraldehyde 3-phosphate
-
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C
16
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
24
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
160
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
190
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
220
D-glyceraldehyde 3-phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
261
D-glyceraldehyde 3-phosphate
-
30°C, 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 23°C
600
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
750
D-glyceraldehyde 3-phosphate
-
mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C
750
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C
750
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
770
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
833
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
833
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C
1100
D-glyceraldehyde 3-phosphate
-
25°C, 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
1666
D-glyceraldehyde 3-phosphate
-
presence of 2-carboxyethyl methanethiosulfonate
2100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
2100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
2100
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
2170
D-glyceraldehyde 3-phosphate
-
in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C
2170
D-glyceraldehyde 3-phosphate
-
mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C
2450
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, tetrameric enzyme form
3100
D-glyceraldehyde 3-phosphate
-
25°C, pH 7.4, mutant enzyme C126A
3166
D-glyceraldehyde 3-phosphate
-
presence of methyl methanethiosulfonate
3200
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
3372
D-glyceraldehyde 3-phosphate
in 100 mM triethanolamine (pH 7.4), at 25°C
4160
D-glyceraldehyde 3-phosphate
-
mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C
4300
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25°C
4300
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
4467
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
4500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
5000
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C
5000
D-glyceraldehyde 3-phosphate
-
in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C
5167
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C
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, 25°C
7300
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
0.25
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
4.7
dihydroxyacetone phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
6.5
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
8
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
300
dihydroxyacetone phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
300
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
300
dihydroxyacetone phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
340
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
D-glyceraldehyde 3-phosphate
-
mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C
0.9
D-glyceraldehyde 3-phosphate
-
mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C
59
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
84
D-glyceraldehyde 3-phosphate
-
mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C
120
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
160
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
260
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
280
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
520
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
540
D-glyceraldehyde 3-phosphate
-
mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C
1500
D-glyceraldehyde 3-phosphate
-
mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C
1933
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
3250
D-glyceraldehyde 3-phosphate
-
mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication
6600
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C
8400
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C
8400
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
8400
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C
10500
D-glyceraldehyde 3-phosphate
-
in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C