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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P00943

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This record set is specific for:
Geobacillus stearothermophilus
UNIPROT: P00943 not found.
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Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
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 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bromohydroxyacetone phosphate
suicide inhibitor
DL-glycidol phosphate
suicide inhibitor
Phosphoglycolate
-
2-phosphoglycolate
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPIS_GEOSE
253
0
27206
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
2 * 27000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
X-ray crystallography, only the TIM dimer is fully active
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
-
triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H12N
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 64°C compared to 68°C for the wild-type enzyme
H12N/K13G
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 37°C compared to 68°C for the wild-type enzyme
H13G
-
mutant enzyme with decreased thermal stability compared to wild-type enzyme. Half-life of 11.5 min at 51°C compared to 68°C for the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
22°C, stable indefinitely
2558
8.1
-
22°C, stable indefinitely
2558
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
pH 7, stable indefinitely
37
-
half-life of mutant enzyme H12N/K13G is 11.5 min
51
-
half-life of mutant enzyme H13G is 11.5 min
60
-
pH 8.1, half-life: 4 h
64
-
half-life of mutant enzyme H12N is 11.5 min
68
-
half-life of wild-type recombinant enzyme is 11.5 min
additional information
-
Lys13 plays a crucial role in the functional adaptation of the thermophilic enzyme to high temperatures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes H12N, H13G and H12N/K13G
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fahey, R.C.; Kolb, E.; Harris, J.I.
Triose phosphate isomerase from Bacillus stearothermophilus
Biochem. J.
124
77P
1971
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Artavanis-Tsakonas, S.; Harris, J.I.
Primary structure of triosephosphate isomerase from Bacillus stearothermophilus
Eur. J. Biochem.
108
599-611
1980
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Delboni, L.F.; Mande, S.C.; Rentier-Delrue, F.; Mainfroid, V.; Turley, S.; Vellieux, F.M.; Martial, J.A.; Hol, W.G.
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearotherophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions
Protein Sci.
4
2594-2604
1995
Geobacillus stearothermophilus
Manually annotated by BRENDA team
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
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