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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Moritella marina and UniProt Accession P50921

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Moritella marina
UNIPROT: P50921 not found.
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The taxonomic range for the selected organisms is: Moritella marina
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
2-Phosphoglycolate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 4.8
D-glyceraldehyde 3-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4667 - 7000
D-glyceraldehyde 3-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
89 - 101
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
comparison of Saccharomyces cerevisiae and Moritella marina enzymes to evaluate the temperature dependence of the activation free energy for differently adapted triosephosphate isomerases. Moritella marina TpiA displays a shift in enthalpy-entropy balance characteristic for cold-adapted proteins, due to a few surface-exposed protein loops that show differential mobilities in the two enzymes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPIS_MORMI
256
0
26740
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
X-ray crystallography, only the TIM dimer is fully active
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex, at 2.7 A resolution
-
hanging drop vapor diffusion method. Crystal structure of the enzyme-sulfate complex and the enzyme-2-phosphoglycolate complex at a 2.7 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A238S
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
half-life of wild-type enzyme: 58 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzyme A238S
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alvarez, M.; Zeelen, J.P.; Mainfroid, V.; Rentier-Delrue, F.; Martial, J.A.; Wyns, L.; Wierenga, R.K.; Maes, D.
Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus
J. Biol. Chem.
273
2199-2206
1998
Escherichia coli, Moritella marina
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
Aqvist, J.
Cold adaptation of triosephosphate isomerase
Biochemistry
56
4169-4176
2017
Saccharomyces cerevisiae (P00942), Saccharomyces cerevisiae, Moritella marina (P50921), Moritella marina, Saccharomyces cerevisiae 288c (P00942)
Manually annotated by BRENDA team