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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Thermotoga maritima and UniProt Accession P36204

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Thermotoga maritima
UNIPROT: P36204 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
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
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CP 25
-
-
-
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D-glyceraldehyde-3-phosphate ketol-isomerase
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-
-
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Isomerase, triose phosphate
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-
-
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Lactacin B inducer protein
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-
-
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monoTIM
-
-
-
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PfTIM
-
-
-
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Phosphotriose isomerase
-
-
-
-
TIM
-
-
-
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Triose phosphate isomerase
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-
-
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Triose phosphate mutase
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-
-
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Triose phosphoisomerase
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-
-
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Triosephosphate isomerase
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-
-
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Triosephosphate mutase
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-
-
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vTIM
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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-
-
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intramolecular oxidoreduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bromohydroxyacetone phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
optimum is near pH 8.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
X-ray crystallography, only the TIM dimer is fully active
tetramer
assembled as a dimer of dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H12N/K13G
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mutant enzyme shows increases thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 96°C compared to 94°C of the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzyme H12N/K13G
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alvarez, M.; Wouters, J.; Maes, D.; Mainfroid, V.; Rentier-Delrue, F.; Wyns, L.; Depiereux, E.; Martial, J.A.
Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures
J. Biol. Chem.
274
19181-19187
1999
Geobacillus stearothermophilus, Thermotoga maritima
Manually annotated by BRENDA team
Maes, D.; Zeelen, J.P.; Thanki, N.; Beaucamp, N.; Alvarez, M.; Thi, M.H.; Backmann, J.; Martial, J.A.; Wyns, L.; Jaenicke, R.; Wierenga, R.K.
The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures
Proteins Struct. Funct. Genet.
37
441-453
1999
Thermotoga maritima (P36204), Thermotoga maritima
Manually annotated by BRENDA team
Sleutel, M.; Vanhee, C.; Van de Weerdt, C.; Decanniere, K.; Maes, D.; Wyns, L.; Willaert, R.
The role of surface diffusion in the growth mechanism of triosephosphate isomerase crystals
Cryst. Growth Des.
8
1173-1180
2008
Thermotoga maritima (P36204)
-
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