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Information on EC 2.7.1.28 - triokinase and Organism(s) Homo sapiens

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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
triokinase, triose kinase, htkfc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-triokinase
-
-
-
-
kinase, trio (phosphorylating)
-
-
-
-
triokinase/FMN cyclase
-
triose kinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-glyceraldehyde 3-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-65-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
show the reaction diagram
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
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
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
show the reaction diagram
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00574 - 0.183
ATP
0.0071 - 0.0181
D-glyceraldehyde
0.0099 - 0.0663
dihydroxyacetone
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 4.59
ATP
0.16 - 4.83
D-glyceraldehyde
0.13 - 5
dihydroxyacetone
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 10.5
ATP
1.2 - 27.5
D-glyceraldehyde
7.6 - 321
dihydroxyacetone
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
enzyme TKFC is widely expressed with highest expression noted in the liver and small intestine
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
the dual association of fructose with metabolic syndrome and intolerance is controlled by triose kinase (TK) through the metabolic bifurcation of fructose toward oxidative versus lipogenic routes. Fructose is catabolized at a much higher rate than glucose, and triose kinase (TK) couples fructolysis with lipogenesis metabolically and transcriptionally. Triose kinase controls the fate of fructose metabolism glyceraldehyde (GA) represents the only branch point in fructose metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TKFC_HUMAN
575
0
58947
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C404A
the mutant shows reduced activity compared to the wild type enzyme
G445S
naturally occuring mutation and site-directed mutagenesis, almost inactive mutant
H221A
inactive
K204A
the mutant shows reduced activity compared to the wild type enzyme
R543I
naturally occuring mutation and site-directed mutagenesis, almost inactive mutant
S446A
the mutant shows reduced activity compared to the wild type enzyme
T112A
the mutant shows reduced activity compared to the wild type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TKFC, DNA and amino acid sequence determination and analysis, genotyping, sequence comparisons, recombinant expression of human TKFC mutant variants in Saccharomyces cerevisiae cells, recombinant expression of wild-type and mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rodrigues, J.R.; Couto, A.; Cabezas, A.; Pinto, R.M.; Ribeiro, J.M.; Canales, J.; Costas, M.J.; Cameselle, J.C.
Bifunctional homodimeric triokinase/FMN cyclase: contribution of protein domains to the activities of the human enzyme and molecular dynamics simulation of domain movements
J. Biol. Chem.
289
10620-10636
2014
Homo sapiens (Q3LXA3), Homo sapiens
Manually annotated by BRENDA team
Wortmann, S.; Meunier, B.; Mestek-Boukhibar, L.; van den Broek, F.; Maldonado, E.; Clement, E.; Weghuber, D.; Spenger, J.; Jaros, Z.; Taha, F.; Yue, W.; Heales, S.; Davison, J.; Mayr, J.; Rahman, S.
Bi-allelic variants in TKFC encoding triokinase/FMN cyclase are associated with cataracts and multisystem disease
Am. J. Hum. Genet.
106
256-263
2020
Homo sapiens (Q3LXA3)
Manually annotated by BRENDA team
Liu, L.; Li, T.; Liao, Y.; Wang, Y.; Gao, Y.; Hu, H.; Huang, H.; Wu, F.; Chen, Y.G.; Xu, S.; Fu, S.
Triose kinase controls the lipogenic potential of fructose and dietary tolerance
Cell Metab.
32
1-14
2020
Homo sapiens (Q3LXA3), Homo sapiens, Mus musculus (Q8VC30), Mus musculus C57BL/6J (Q8VC30)
Manually annotated by BRENDA team
Rodrigues, J.R.; Cameselle, J.C.; Cabezas, A.; Ribeiro, J.M.
Closure of the human TKFC active site comparison of the apoenzyme and the complexes formed with either triokinase or FMN cyclase substrates
Int. J. Mol. Sci.
20
1099
2019
Homo sapiens (Q3LXA3), Homo sapiens
Manually annotated by BRENDA team