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Information on EC 2.2.1.1 - transketolase and Organism(s) Plasmodium falciparum

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EC Tree
     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.1 transketolase
IUBMB Comments
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
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Plasmodium falciparum
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Word Map
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
Synonyms
transketolase, tktl1, transketolase a, transketolase-like 1, tktl-1, transketolase-like-1, tktl2, transketolase-like enzyme 1, transketolase-like-2, tkt10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycolaldehydetransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
keto group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-48-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
fructose-6-phosphate + hydroxypyruvate
?
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-hydroxyphenylpyruvate
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potent inhibitor when hydroxypyruvate is used as a substrate, whereas noncompetitive inhibition with fructose-6-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.25
fructose-6-phosphate
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-
4.78
Hydroxypyruvate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.305
p-hydroxyphenylpyruvate
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with hydroxypyruvate as substrate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
clone NF54
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
late trophozoite stage
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
6 * 70000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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6 * 70000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on Ni2+-NTA resin and by ammonium sulfate precipitation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli BL21(DE3)Rosetta cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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Plasmodium falciparum transketolase shows low homology with the host enzyme, thus may serve as a novel and promising target for designing inhibitors with anti-malarial activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Joshi, S.; Singh, A.R.; Kumar, A.; Misra, P.C.; Siddiqi, M.I.; Saxena, J.K.
Molecular cloning and characterization of Plasmodium falciparum transketolase
Mol. Biochem. Parasitol.
160
32-41
2008
Plasmodium falciparum
Manually annotated by BRENDA team