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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Gallus gallus and UniProt Accession P00940
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EC Tree
5.3.1.1 triose-phosphate isomeraseSpecify your search results
Word Map
- 5.3.1.1
- giardia
-
assemblage
- aldolase
- duodenalis
- dihydroxyacetone
- enolase
- phosphoglycerate
-
zoonotic
-
barrel
-
fecal
- trypanosoma
-
multilocus
- fructose
- giardiasis
- dhap
- cryptosporidium
- brucei
-
protozoan
- isomerases
- gapdh
-
province
- cysts
- malate
-
stool
- lamblia
- methylglyoxal
-
phosphofructokinase
- cruzi
- schistosoma
-
enediolate
- 2-phosphoglycolate
- parvum
-
hemolytic
- intestinalis
- fructose-1,6-bisphosphate
-
deamidation
- alpha-enolase
- 1,6-bisphosphate
-
glucosephosphate
-
tim-barrel
-
hungarian
- hominis
- phosphite
-
dianion
-
phosphoglucose
- glycosomes
-
enzymopathy
-
fructose-bisphosphate
-
ige-binding
-
subgenotype
- diagnostics
- synthesis
- analysis
- biofuel production
- medicine
The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
triosephosphate isomerase, triose phosphate isomerase, triose-phosphate isomerase, tctim, pftim, gltim, monotim, pfutim, cp 25, cytoplasmic tpi, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CP 25
-
-
-
-
D-glyceraldehyde-3-phosphate ketol-isomerase
-
-
-
-
Isomerase, triose phosphate
-
-
-
-
Lactacin B inducer protein
-
-
-
-
monoTIM
-
-
-
-
PfTIM
-
-
-
-
Phosphotriose isomerase
-
-
-
-
TIM
Triose phosphate isomerase
-
-
-
-
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
TIM
-
-
-
-
Triosephosphate isomerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
CAS REGISTRY NUMBER
COMMENTARY
9023-78-3
-
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
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
glycolaldehyde
?
-
TIM-catalyzed reactions of glycolaldehyde are activated by phosphite dianion, kinetics, overview
-
-
?
NATURAL SUBSTRATE
NATURAL 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.29
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 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
0.59
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
16
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
261
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.6, mutant enzyme K174G/T175G/A176G
3200
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
0.25
dihydroxyacetone phosphate
-
30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G
8
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
340
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
59
D-glyceraldehyde 3-phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
11000
D-glyceraldehyde 3-phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
2
dihydroxyacetone phosphate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
580
dihydroxyacetone phosphate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
2-Phosphoglycolate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
2.3
2-Phosphoglycolate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
3.8
arsenate
-
mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
9.6
arsenate
-
wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TPIS_CHICK
248
0
26620
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
simulation of both dimeric and monomeric (isolated from dimer) forms in explicit water at 27°C 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
crystal structure of the recombinant enzyme complexed with phosphoglycolohydroxamate, at 1.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V167P/W168E
loop replacement mutant, 23000fold decrease in kcat/Km value. Mutations result in large displacement of the side chain of E168 from that for W168 in wild-type. Binding of glycerol 3-phosphate results in chemical shift changes for nuclei at the active site that are smaller than those of wild-type
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
L7RM
-
the mutant exhibits a 200fold decrease in kcat/Km for isomerization of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The mutant exhibits a 25fold decrease in kcat/Km for deprotonation of glycolaldehyde catalyzed by free enzyme. The mutation has little effect on the observed and intrinsic phosphodianion binding energy and only a modest effect on phosphite dianion activation of the enzyme
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Esnouf, M.P.; Harris, R.P.; McVittie, J.D.
Triosephosphate isomerase from chicken and rabbit muscle
Methods Enzymol.
89
579-583
1982
Gallus gallus, Oryctolagus cuniculus
Blacklow, S.C.; Raines, R.T.; Lim, W.A.; Zamore, Ph.D.; Knowles, J.R.
Triosephosphate isomerase catalysis is diffusion controlled
Biochemistry
27
1158-1167
1988
Gallus gallus
Carza-Ramos, G.; Perez-Montfort, R.; Rojo-Dominguez, A.; de Gomez-Puyou, M.T.; Gomez-Puyou, A.
Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase
Eur. J. Biochem.
241
114-120
1996
Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Schizosaccharomyces pombe
Zhang, Z.; Sugio, S.; Komives, E.A.; Liu, K.D.; Knowles, J.R.; Petsko, G.A.; Ringe, D.
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution
Biochemistry
33
2830-2837
1994
Gallus gallus
Xiang, J.; Jung, J.Y.; Sampson, N.S.
Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase
Biochemistry
43
11436-11445
2004
Gallus gallus
Cansu, S.; Doruker, P.
Dimerization affects collective dynamics of triosephosphate isomerase
Biochemistry
47
1358-1368
2008
Gallus gallus (P00940)
Shi, Y.; Liu, J.H.; Zhang, H.J.; Ding, Y.
Equilibrium unfolding mechanism of chicken muscle triose phosphate isomerase
Protein Pept. Lett.
15
365-370
2008
Gallus gallus
Wang, Y.; Berlow, R.B.; Loria, J.P.
Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase
Biochemistry
48
4548-4556
2009
Gallus gallus
Go, M.K.; Amyes, T.L.; Richard, J.P.
Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D2O
Biochemistry
48
5769-5778
2009
Gallus gallus
Wierenga, R.K.; Kapetaniou, E.G.; Venkatesan, R.
Triosephosphate isomerase: a highly evolved biocatalyst
Cell. Mol. Life Sci.
67
3961-3982
2010
Entamoeba histolytica (O02611), Oryctolagus cuniculus (P00939), Gallus gallus (P00940), Saccharomyces cerevisiae (P00942), Geobacillus stearothermophilus (P00943), Trypanosoma brucei brucei (P04789), Escherichia coli (P0A858), Giardia intestinalis (P36186), Thermotoga maritima (P36204), Leishmania mexicana (P48499), Moritella marina (P50921), Trypanosoma cruzi (P52270), Helicobacter pylori (P56076), Homo sapiens (P60174), Pyrococcus woesei (P62003), Mycobacterium tuberculosis (P9WG43), Plasmodium falciparum (Q07412), Caenorhabditis elegans (Q10657), Methanocaldococcus jannaschii (Q58923), Bartonella henselae (Q8L1Z5), Tenebrio molitor (Q8MPF2), Thermoproteus tenax (Q8NKN9), Mycobacterium tuberculosis H37Rv (P9WG43)
Zhai, X.; Amyes, T.L.; Wierenga, R.K.; Loria, J.P.; Richard, J.P.
Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase
Biochemistry
52
5928-5940
2013
Gallus gallus, Trypanosoma brucei brucei
Zhai, X.; Go, M.K.; ODonoghue, A.C.; Amyes, T.L.; Pegan, S.D.; Wang, Y.; Loria, J.P.; Mesecar, A.D.; Richard, J.P.
Enzyme architecture the effect of replacement and deletion mutations of loop 6 on catalysis by triosephosphate isomerase
Biochemistry
53
3486-3501
2014
Gallus gallus (P00940), Gallus gallus
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