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Information on EC 5.3.1.1 - triose-phosphate isomerase and Organism(s) Staphylococcus aureus and UniProt Accession Q6GIL6

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Staphylococcus aureus
UNIPROT: Q6GIL6 not found.
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The taxonomic range for the selected organisms is: Staphylococcus aureus
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
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
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
dihydroxyacetone phosphate
D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
mannobiose
-
-
Mannopentaose
-
-
Mannotetraose
-
-
Mannotriose
-
docking simulation
additional information
-
stronger inhibition by alpha-(1,3)-mannooligosaccharides than with triose, binding constants, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
-
purified native enzyme
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
-
TPI of Staphylococcus aureus is a candidate adhesion molecule for the interaction between the bacterium and the fungal pathogen Cryptococcus neoformans. TPI may recognize the mannan backbone of glucuronoxylomannan of Cryptococcus neoformans
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, about, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, about, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme alone and in complex with various phosphate containing ligands like glycerol 3-phosphate, glycerol 2-phosphate, 3-phosphoglyceric acid, and 2-phosphoglyceric acid, hanging drop vapor diffusion method
purified recombinant enzyme by hanging drop vapour diffusion method, from 1.6 M trisodium citrate dihydrate, pH 6.5, X-ray diffraction structure determination and analysis at1.9 A resolution, modeling
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 2400fold from cell surface by hydrophobic interaction and anion exchange chromatography, followed by adsorption chromatography
-
recombinant enzyme from Escherichia coli strain M15 to homogeneity by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of the enzyme in Escherichia coli strain M15
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mukherjee, S.; Dutta, D.; Saha, B.; Das, A.K.
Expression, purification, crystallization and preliminary X-ray diffraction studies of triosephosphate isomerase from methicillin-resistant Staphylococcus aureus (MRSA252)
Acta Crystallogr. Sect. F
65
398-401
2009
Staphylococcus aureus
Manually annotated by BRENDA team
Furuya, H.; Ikeda, R.
Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and alpha-(1->3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans
Microbiology
155
2707-2713
2009
Staphylococcus aureus, Staphylococcus aureus RN4220
Manually annotated by BRENDA team
Mukherjee, S.; Roychowdhury, A.; Dutta, D.; Das, A.K.
Crystal structures of triosephosphate isomerase from methicillin resistant Staphylococcus aureus MRSA252 provide structural insights into novel modes of ligand binding and unique conformations of catalytic loop
Biochimie
94
2532-2544
2012
Staphylococcus aureus (Q6GIL6), Staphylococcus aureus, Staphylococcus aureus MRSA252 (Q6GIL6), Staphylococcus aureus MRSA252
Manually annotated by BRENDA team