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Information on EC 2.7.1.28 - triokinase
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2.7.1.28 triokinaseSpecify your search results
Word Map
- 2.7.1.28
- fructose
- dihydroxyacetone
- fructokinase
- ketohexokinase
-
gluconeogenesis
- glycerate
-
fructolysis
-
d-glyceric
- fructose-1-phosphate
-
fructose-metabolizing
-
gluconeogenic
-
malabsorption
- glucose-6-phosphatase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
triokinase, triose kinase, htkfc, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-triokinase
-
-
-
-
dAK
kinase, trio (phosphorylating)
-
-
-
-
TKFC
triose kinase
triose kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-glyceraldehyde 3-phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9030-65-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + D-glyceraldehyde
GDP + D-glyceraldehyde-3-phosphate
-
10% of the activity with ATP
-
?
ITP + D-glyceraldehyde
IDP + D-glyceraldehyde-3-phosphate
-
14% of the activity with ATP
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
-
-
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
-
-
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde-3-phosphate
-
enzyme of Hers' pathway for fructose metabolism, main pathway for D-glyceraldehyde metabolism in liver
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
2.5fold higher activity than with D-glyceraldehyde
-
?
ATP + glyceraldehyde
ADP + D-glyceraldehyde-3-phosphate
-
D-glyceraldehyde and DL-glyceraldehyde
-
?
additional information
?
-
no activity with glycolaldehyde and glycerol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
-
-
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
-
-
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde-3-phosphate
-
enzyme of Hers' pathway for fructose metabolism, main pathway for D-glyceraldehyde metabolism in liver
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
free ADP, 0.5 mM, 50% inhibition, competitive to MgATP2-, noncompetitive to D-glyceraldehyde
ATP
-
free ATP, 1.5 mM, 50% inhibition, competitive to MgATP2-, noncompetitive to D-glyceraldehyde
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
A selective system for hepatoma cells producing gluconeogenic enzymes.
triokinase deficiency
D-glyceric acidemia: an inborn error associated with fructose metabolism.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00574
ATP
mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.0352
ATP
mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
0.0432
ATP
wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.0624
ATP
wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
0.0637
ATP
mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.0696
ATP
mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
0.0806
ATP
mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.0853
ATP
mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
0.0996
ATP
mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.183
ATP
mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
ATP
mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.16
ATP
mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
0.5
ATP
mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
0.66
ATP
mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
1.7
ATP
mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
2.1
ATP
mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C
2.17
ATP
mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
2.34
ATP
mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
3.94
ATP
wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
4.59
ATP
wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
ATP
mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
0.64
ATP
mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
1.15
ATP
mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C
1.9
ATP
mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
2.18
ATP
mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
2.4
ATP
mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
2.6
ATP
mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
4.2
ATP
mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
6.3
ATP
wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C
10.5
ATP
wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0024
-
activity in the liver of female rats fed with fructose diet containing copper-adequate
0.0034
-
activity in the liver of male rats fed with fructose diet containing copper-adequate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
caloric restricted young (3 months) and old (30 months) male C57BL/6J mice
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
enzyme TKFC is widely expressed with highest expression noted in the liver and small intestine
brenda
-
in young caloric restricted mice the triokinase activity is unchanged compared with control mice. In old caloric restricted mice the triokinase activity is increased about 16% compared to the control group. Comparison between young and old caloric restricted mice, the old have a significantly increased triokinase activity in hepatic tissue (enzyme assay is perfomed at 25°C).
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
hTKFC is functionally and structurally similar to Citrobacter sp. DHA kinase
evolution
triose kinase polymorphism demarcates the routes of human migration out of Africa. A nonsynonymous TK allele (rs2260655_A) segregated during human migration out of Africa behaves as TK null for its inability to rescue fructose toxicity and increase hepatic triglyceride accumulation
malfunction
the analyzed TKFC homozygous variants are located within the FMN lyase domain. Functional assays in yeast support the deleterious effect of these variants on protein function. Shared phenotypes between affected individuals with TKFC deficiency include cataracts and developmental delay, associated with cerebellar hypoplasia in one case. Further complications observed in two affected individuals included liver dysfunction and microcytic anemia, while one had fatal cardiomyopathy with lactic acidosis following a febrile illness. Deficiency of TKFC causes disruption of endogenous fructose metabolism leading to generation of by-products that can cause cataract. Deficiency of TKFC leads to impaired innate immunity in response to viral illness, which may explain the fatal illness observed in the most severely affected individual. Phenotypic analyses, oveerview
malfunction
triose kinase deficiency causes oxidative stress and dietary fructose intolerance. In the absence of TK, fructose oxidation is accelerated through the activation of aldehyde dehydrogenase (ALDH) and serine biosynthesis, accompanied by increased oxidative stress and fructose aversion. A nonsynonymous TK allele (rs2260655_A) segregated behaves as TK null for its inability to rescue fructose toxicity and increase hepatic triglyceride accumulation
malfunction
triose kinase deficiency causes oxidative stress and dietary fructose intolerance. In the absence of TK, fructose oxidation is accelerated through the activation of aldehyde dehydrogenase (ALDH) and serine biosynthesis, accompanied by increased oxidative stress and fructose aversion. A nonsynonymous TK allele (rs2260655_A) segregated behaves as TK null for its inability to rescue fructose toxicity and increase hepatic triglyceride accumulation. Deletion of Tk nearly doubles the rate of fructose oxidation, but not the rate of lactate secretion providing an initial indication that TK deficiency may differentially modulate fructose metabolism downstream of glyceraldehyde. Enzyme TK deficiency sensitizes cells to fructose toxicity. TK-deficient mice develop fructose avoidance. TK deficiency reduces hepatic triglyceride accumulation
malfunction
-
triose kinase deficiency causes oxidative stress and dietary fructose intolerance. In the absence of TK, fructose oxidation is accelerated through the activation of aldehyde dehydrogenase (ALDH) and serine biosynthesis, accompanied by increased oxidative stress and fructose aversion. A nonsynonymous TK allele (rs2260655_A) segregated behaves as TK null for its inability to rescue fructose toxicity and increase hepatic triglyceride accumulation. Deletion of Tk nearly doubles the rate of fructose oxidation, but not the rate of lactate secretion providing an initial indication that TK deficiency may differentially modulate fructose metabolism downstream of glyceraldehyde. Enzyme TK deficiency sensitizes cells to fructose toxicity. TK-deficient mice develop fructose avoidance. TK deficiency reduces hepatic triglyceride accumulation
-
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
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
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
human triokinase/flavin mononucleotide (FMN) cyclase (hTKFC) is a bifunctional enzyme which catalyzes the adenosine triphosphate (ATP)-dependent phosphorylation of D-glyceraldehyde (GA) and dihydroxyacetone (DHA), and also the Mn2+-dependent splitting of flavin adenine dinucleotide (FAD) by an internal cyclizing reaction that forms adenosine monophosphate (AMP) and riboflavin 4',5'-phosphate or cyclic FMN
physiological function
TKFC encodes a bifunctional protein that has been annotated as a homodimeric triokinase and FMN cyclase. Triokinase is a component of the fructose metabolism pathway. Role of TKFC in regulating innate antiviral immunity through suppression of MDA5
physiological function
triose kinase (TK) constrains fructose oxidation in favor of lipogenic metabolism. Hyperglycemia activates fructolysis through TK to stimulate hepatic lipogenesis. 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. TK is also required by the endogenous fructolysis pathway to drive lipogenesis and hepatic triglyceride accumulation under high-fat diet and leptin-deficient conditions
physiological function
triose kinase (TK) constrains fructose oxidation in favor of lipogenic metabolism. Hyperglycemia activates fructolysis through TK to stimulate hepatic lipogenesis. 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. TK is also required by the endogenous fructolysis pathway to drive lipogenesis and hepatic triglyceride accumulation under high-fat diet and leptin-deficient conditions
physiological function
-
triose kinase (TK) constrains fructose oxidation in favor of lipogenic metabolism. Hyperglycemia activates fructolysis through TK to stimulate hepatic lipogenesis. 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. TK is also required by the endogenous fructolysis pathway to drive lipogenesis and hepatic triglyceride accumulation under high-fat diet and leptin-deficient conditions
-
additional information
study of the flexibility of dimeric hTKFC starting with its active sites in an open conformation, molecular dynamics simulation of the structural model of hTKFC containing the kinase substrates dihydroxyacetone (DHA covalently bound to His221) and ATP. Enzyme structure homology modelling using the crystal structure of Citrobacter sp. DHA kinase. The normal-mode analysis of hTKFC models confirms the trend of K domains to approach L domains, different modes, overview
additional information
-
study of the flexibility of dimeric hTKFC starting with its active sites in an open conformation, molecular dynamics simulation of the structural model of hTKFC containing the kinase substrates dihydroxyacetone (DHA covalently bound to His221) and ATP. Enzyme structure homology modelling using the crystal structure of Citrobacter sp. DHA kinase. The normal-mode analysis of hTKFC models confirms the trend of K domains to approach L domains, different modes, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DHAK_DICDI
648
0
71006
Swiss-Prot
other Location (Reliability: 2)
TKFC_BOVIN
578
0
59124
Swiss-Prot
other Location (Reliability: 2)
TKFC_HUMAN
575
0
58947
Swiss-Prot
other Location (Reliability: 2)
TKFC_MOUSE
578
0
59691
Swiss-Prot
other Location (Reliability: 1)
TKFC_PIG
579
0
59234
Swiss-Prot
other Location (Reliability: 2)
TKFC_RAT
578
0
59444
Swiss-Prot
other Location (Reliability: 2)
DAK1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
580
0
62316
Swiss-Prot
other Location (Reliability: 2)
DAK1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
584
0
62207
Swiss-Prot
other Location (Reliability: 2)
DAK2_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
591
0
62127
Swiss-Prot
other Location (Reliability: 5)
DAK2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
591
0
62135
Swiss-Prot
other Location (Reliability: 4)
DAK_PICAN
609
0
65071
Swiss-Prot
other Location (Reliability: 2)
DAK_PICPA
608
0
65312
Swiss-Prot
other Location (Reliability: 3)
A0A2I6PBE1_PICKU
607
0
65499
TrEMBL
other Location (Reliability: 2)
A0A445JV87_GLYSO
650
0
67923
TrEMBL
Chloroplast (Reliability: 2)
A0A8J5BQ76_9ASCO
572
0
60153
TrEMBL
other Location (Reliability: 2)
A0A1Z5JW24_FISSO
593
0
62054
TrEMBL
other Location (Reliability: 1)
A0A7R8H914_LEPSM
228
0
24215
TrEMBL
other Location (Reliability: 1)
A0A8J5BHD5_9ASCO
585
0
62361
TrEMBL
other Location (Reliability: 1)
A0A8J5BQP4_9ASCO
566
0
60196
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6J8AAI1_MYTCO
218
0
23243
TrEMBL
other Location (Reliability: 1)
A0A1S7RCK4_9HYPH
562
0
57191
TrEMBL
-
A0A445JV89_GLYSO
618
0
64695
TrEMBL
Chloroplast (Reliability: 2)
A0A8J5BK45_9ASCO
563
0
59853
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0L0HQW3_SPIPD
Spizellomyces punctatus (strain DAOM BR117)
769
0
82707
TrEMBL
other Location (Reliability: 1)
A0A1Z5K6L6_FISSO
595
0
62597
TrEMBL
other Location (Reliability: 1)
Q9HFC5_ZYGRO
587
0
61752
TrEMBL
other Location (Reliability: 2)
A0A0B2SF64_GLYSO
592
0
61260
TrEMBL
other Location (Reliability: 2)
A0A445JV63_GLYSO
593
0
62241
TrEMBL
Chloroplast (Reliability: 2)
A0A812B4W4_SEPPH
227
0
24093
TrEMBL
other Location (Reliability: 1)
A0A3M7MP61_9EURO
1388
1
151725
TrEMBL
Mitochondrion (Reliability: 3)
A0A8J5BP46_9ASCO
571
0
60107
TrEMBL
other Location (Reliability: 2)
A0A5B6Z9Z2_DAVIN
594
0
61783
TrEMBL
other Location (Reliability: 2)
A0A445JV80_GLYSO
654
0
68392
TrEMBL
Chloroplast (Reliability: 2)
A0A445JV36_GLYSO
592
0
61226
TrEMBL
other Location (Reliability: 2)
A0A5B6Z761_DAVIN
566
0
58924
TrEMBL
other Location (Reliability: 2)
W1QF08_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
609
0
65034
TrEMBL
other Location (Reliability: 2)
A0A8J5ENV4_9ASCO
586
0
62614
TrEMBL
other Location (Reliability: 1)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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