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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Homo sapiens and UniProt Accession P60174

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Homo sapiens
UNIPROT: P60174 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triosephosphate isomerase
-
CP 25
-
-
-
-
D-glyceraldehyde-3-phosphate ketol-isomerase
-
-
-
-
Isomerase, triose phosphate
-
-
-
-
Lactacin B inducer protein
-
-
-
-
monoTIM
-
-
-
-
PfTIM
-
-
-
-
Phosphotriose isomerase
-
-
-
-
TPI1
-
-
Triose phosphate isomerase
-
-
-
-
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-78-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
r
D-glyceraldehyde 3-phosphate
dihydroxyacetone 3-phosphate
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate
dihydroxyacetone phosphate
show the reaction diagram
-
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme may be involved in integrin alphaIIb/beta3-mediated platelet function
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bromohydroxyacetone phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
1,2,4-thiadiazole
-
59% inhibition at 0.1 mM
AsO43-
-
competitive
ATP
-
-
Chloroacetol phosphate
-
-
D-alpha-glycerophosphate
-
competitive
phosphoenolpyruvate
-
competitive
Phosphoglycolate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 1.373
D-glyceraldehyde 3-phosphate
0.26 - 1.5
glycerone phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.5
phosphoenolpyruvate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.154 - 0.57
phosphoenolpyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10240
-
-
2397
-
-
5360
-
isoenzyme A
6900
-
isoenzyme B
8060
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
optimum is near pH 8.0
7 - 9.5
-
-
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
gastric cancer cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
serum
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
-
the enzyme is involved in glycolysis
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPIS_HUMAN
249
0
26669
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26500
-
x * 26500, SDS-PAGE
26732
-
2 * 26732, calculated from amino acid sequence
54000
-
gel filtration
56000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
X-ray crystallography, only the TIM dimer is fully active
?
-
x * 26500, SDS-PAGE
dimer
homodimer
-
2 * 26732, calculated from amino acid sequence
additional information
-
in a yeast two-hybrid system, enzyme interacts with integrin alphaIIb cytoplasmic domain and binds weakly to its alphaV tail
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
high resolution structure of crystal form 2 employing the gel-tube method in microgravity
-
triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E104D
I170V
the mutation is asociated with a mild form of TIM deficiency
I170T
-
13% residual activity
I170V
-
5.9% residual activity
K13R
-
mutant is catalytically inactive and largely unstable
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
-
the melting temperature of the active form P1 of TIM is 48°C
64
-
the melting temperature of the active form P2 of TIM is 64°C
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea
-
the enzyme is denatured in buffer with 3 M urea
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant mutant E104D
3 distinct electrophoretic forms: I, II, III
-
3 isoenzymes
-
Ni-NTA agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 in Saccharomyces cerevsiae
-
expression of TPI in Spodoptera frugiperda Sf21 cells using the baculovirus transfection system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is upregulated in lung squamous cell carcinoma
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation into catalytic active enzyme by removal of the dissociating agent
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
triosephosphate isomerase is a serum marker for human lung squamous cell carcinoma
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rozacky, E.E.; Sawyer, T.H.; Barton, R.A.; Gracy, R.W.
Studies on human triosephosphate isomerase. I. Isolation and properties of the enzyme from erythrocytes
Arch. Biochem. Biophys.
146
312-320
1971
Homo sapiens
Manually annotated by BRENDA team
Snyder, R.; Lee, E.W.
Triosephosphate isomerase from human and horse liver
Methods Enzymol.
41B
430-434
1975
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Gracy, R.W.
Triosephosphate isomerase from human erythrocytes
Methods Enzymol.
41B
442-447
1975
Homo sapiens
Manually annotated by BRENDA team
Yuan, P.M.; Dewan, R.N.; Zaun, M.; Thompson, R.E.; Gracy, R.W.
Isolation and characterization of triosephosphate isomerase isozymes from human placenta
Arch. Biochem. Biophys.
198
42-52
1979
Homo sapiens
Manually annotated by BRENDA team
Eber, S.W.; Krietsch, W.K.G.
The isolation and characterization of the multiple forms of human skeletal muscle triosephosphate isomerase
Biochim. Biophys. Acta
614
173-184
1980
Homo sapiens
Manually annotated by BRENDA team
Mande, S.C.; Mainfroid, V.; Kalk, K.H.; Goraj, K.; Martial, J.A.; Hol, W.G.
Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme
Protein Sci.
3
810-821
1994
Homo sapiens
Manually annotated by BRENDA team
Kinoshita, T.; Maruki, R.; Warizaya, M.; Nakajima, H.; Nishimura, S.
Structure of a high-resolution crystal form of human triosephosphate isomerase: Improvement of crystals using the gel-tube method
Acta Crystallogr. Sect. F
F61
346-349
2005
Homo sapiens
Manually annotated by BRENDA team
Liu, Q.Y.; Corjay, M.; Feuerstein, G.Z.; Nambi, P.
Identification and characterization of triosephosphate isomerase that specifically interacts with the integrin alphaIIb cytoplasmic domain
Biochem. Pharmacol.
72
551-557
2006
Homo sapiens
Manually annotated by BRENDA team
Rodriguez-Almazan, C.; Arreola, R.; Rodriguez-Larrea, D.; Aguirre-Lopez, B.; de Gomez-Puyou, M.T.; Perez-Montfort, R.; Costas, M.; Gomez-Puyou, A.; Torres-Larios, A.
Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface
J. Biol. Chem.
283
23254-23263
2008
Homo sapiens (P60174), Homo sapiens
Manually annotated by BRENDA team
Wang, X.; Lu, Y.; Yang, J.; Shi, Y.; Lan, M.; Liu, Z.; Zhai, H.; Fan, D.
Identification of triosephosphate isomerase as an anti-drug resistance agent in human gastric cancer cells using functional proteomic analysis
J. Cancer Res. Clin. Oncol.
134
995-1003
2008
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.Z.; Xiao, Z.F.; Li, C.; Xiao, Z.Q.; Yang, F.; Li, D.J.; Li, M.Y.; Li, F.; Chen, Z.C.
Triosephosphate isomerase and peroxiredoxin 6, two novel serum markers for human lung squamous cell carcinoma
Cancer Sci.
100
2396-2401
2009
Homo sapiens
Manually annotated by BRENDA team
Lee, W.H.; Choi, J.S.; Byun, M.R.; Koo, K.T.; Shin, S.; Lee, S.K.; Surh, Y.J.
Functional inactivation of triosephosphate isomerase through phosphorylation during etoposide-induced apoptosis in HeLa cells: Potential role of Cdk2
Toxicology
278
224-228
2010
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Alvarez, G.; Aguirre-Lopez, B.; Varela, J.; Cabrera, M.; Merlino, A.; Lopez, G.V.; Lavaggi, M.L.; Porcal, W.; Di Maio, R.; Gonzalez, M.; Cerecetto, H.; Cabrera, N.; Perez-Montfort, R.; de Gomez-Puyou, M.T.; Gomez-Puyou, A.
Massive screening yields novel and selective Trypanosoma cruzi triosephosphate isomerase dimer-interface-irreversible inhibitors with anti-trypanosomal activity
Eur. J. Med. Chem.
45
5767-5772
2010
Homo sapiens, Trypanosoma cruzi, Trypanosoma cruzi T2
Manually annotated by BRENDA team
Aguirre, B.; Costas, M.; Cabrera, N.; Mendoza-Hernandez, G.; Helseth, D.L.; Fernandez, P.; Tuena de Gomez-Puyou, M.; Perez-Montfort, R.; Torres-Larios, A.; Gomez Puyou, A.
A Ribosomal misincorporation of Lys for Arg in human triosephosphate isomerase expressed in Escherichia coli gives rise to two protein populations
PLoS ONE
6
e21035
2011
Homo sapiens
Manually annotated by BRENDA team
Jiang, H.; Ma, N.; Shang, Y.; Zhou, W.; Chen, T.; Guan, D.; Li, J.; Wang, J.; Zhang, E.; Feng, Y.; Yin, F.; Yuan, Y.; Fang, Y.; Qiu, L.; Xie, D.; Wei, D.
Triosephosphate isomerase 1 suppresses growth, migration and invasion of hepatocellular carcinoma cells
Biochem. Biophys. Res. Commun.
482
1048-1053
2017
Homo sapiens
Manually annotated by BRENDA team
Gruening, N.M.; Du, D.; Keller, M.A.; Luisi, B.F.; Ralser, M.
Inhibition of triosephosphate isomerase by phosphoenolpyruvate in the feedback-regulation of glycolysis
Open biology
4
130232
2014
Homo sapiens, Oryctolagus cuniculus (P00939)
Manually annotated by BRENDA team