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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Leishmania mexicana and UniProt Accession P48499

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Leishmania mexicana
UNIPROT: P48499 not found.
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The taxonomic range for the selected organisms is: Leishmania mexicana
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
-
-
-
-
TIM
-
-
-
-
Triose phosphate isomerase
-
-
-
-
Triose phosphate mutase
-
-
-
-
Triose phosphoisomerase
-
-
-
-
Triosephosphate isomerase
-
-
-
-
Triosephosphate mutase
-
-
-
-
vTIM
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
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
Glycerone phosphate
show the reaction diagram
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
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 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
the reaction is essential in vivo
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
-
bromohydroxyacetone phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
Phosphoglycolohydroxamate
the reaction-intermediate analogue binds to the active site with two hydrogen-bonding interactions between PGH and the Glu167 side-chain oxygen atoms
2,2'-methylenebis(1,3-benzothiazole)
-
irreversible inactivation
6,6'-bi-1,3-benzothiazole-2,2'-diamine
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irreversible inactivation. Not inhibitory on human, yeast, chicken, Plasmodium falciparum, and Entamoeba histolytica 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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 0.9
D-glyceraldehyde 3-phosphate
1.1 - 1.3
glycerone phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4000 - 4170
D-glyceraldehyde 3-phosphate
367
glycerone phosphate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
2-(N-formyl-N-hydroxy)-aminoethyl phosphonate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
optimum is near pH 8.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6.0: about 60% of maximal activity, pH 9.0: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPIS_LEIME
251
0
27178
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
2 * 28000, SDS-PAGE
44800
-
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E65Q
the variant of Leishmania mexicana TIM has a much enhanced stability but its catalytic properties are the same as wild-type leishmanial TIM
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
20 h, stable
2585
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
-
stable for at least 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kohl, L.; Callens, M.; Wierenga, R.K.; Opperdoes, F.R.; Michels, P.A.M.
Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein
Eur. J. Biochem.
220
331-338
1994
Leishmania mexicana
Manually annotated by BRENDA team
Ostoa-Saloma, P.; Garza-Ramos, G.; Ramirez, J.; Becker, I.; Berzunza, M.; Landa, A.; Gomez-Puyou, A.; Tuena de Gomez-Puyou, M.; Perez-Montfort, R.
Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi
Eur. J. Biochem.
244
700-705
1997
Leishmania mexicana, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team
Kursula, I.; Partanen, S.; Lambeir, A.M.; Antonov, D.M.; Augustyns, K.; Wierenga, R.K.
Structural determinants for ligand binding and catalysis of triosephosphate isomerase
Eur. J. Biochem.
268
5189-5196
2001
Leishmania mexicana (P48499)
Manually annotated by BRENDA team
Kursula, I.; Wierenga, R.K.
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
J. Biol. Chem.
278
9544-9551
2003
Leishmania mexicana
Manually annotated by BRENDA team
Olivares-Illana, V.; Perez-Montfort, R.; Lopez-Calahorra, F.; Costas, M.; Rodriguez-Romero, A.; Tuena de Gomez-Puyou, M.; Gomez Puyou, A.
Structural differences in triosephosphate isomerase from different species and discovery of a multitrypanosomatid inhibitor
Biochemistry
45
2556-2560
2006
Leishmania mexicana, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team
Alahuhta, M.; Wierenga, R.K.
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism
Proteins
78
1878-1888
2010
Leishmania mexicana (P48499)
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