Information on EC 2.7.1.28 - triokinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.28
-
RECOMMENDED NAME
GeneOntology No.
triokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
-
-
sucrose degradation V (sucrose alpha-glucosidase)
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-glyceraldehyde 3-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-65-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
caloric restricted young (3 months) and old (30 months) male C57BL/6J mice
-
-
Manually annotated by BRENDA team
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 + D-glyceraldehyde
ADP + D-glyceraldehyde-3-phosphate
show the reaction diagram
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
show the reaction diagram
ATP + glyceraldehyde
ADP + D-glyceraldehyde-3-phosphate
show the reaction diagram
GTP + D-glyceraldehyde
GDP + D-glyceraldehyde-3-phosphate
show the reaction diagram
-
10% of the activity with ATP
-
?
ITP + D-glyceraldehyde
IDP + D-glyceraldehyde-3-phosphate
show the reaction diagram
-
14% of the activity with ATP
-
?
additional information
?
-
no activity with glycolaldehyde and glycerol
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q3LXA3
-
-
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde-3-phosphate
show the reaction diagram
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
show the reaction diagram
Q3LXA3
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required in equimolar concentration with ATP
Mn2+
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
MgADP-
-
free, competitive to MgATP2-, noncompetitive to D-glyceraldehyde
additional information
-
not inhibited by Zn2+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00574 - 0.183
ATP
0.0071 - 0.019
D-glyceraldehyde
0.006 - 0.0663
dihydroxyacetone
0.01
glyceraldehyde
-
pH 7.0, 22°C
0.16 - 0.24
MgATP2-
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
4
1.2 - 27.5
D-glyceraldehyde
639
7.6 - 321
dihydroxyacetone
620
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
ADP
-
pH 7.5, 23-24°C
0.38
ATP
-
pH 7.5, 23-24°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0024
-
activity in the liver of female rats fed with fructose diet containing copper-adequate
0.0034
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activity in the liver of male rats fed with fructose diet containing copper-adequate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C404A
the mutant shows reduced activity compared to the wild type enzyme
H221A
inactive
K204A
the mutant shows reduced activity compared to the wild type enzyme
S446A
the mutant shows reduced activity compared to the wild type enzyme
T112A
the mutant shows reduced activity compared to the wild type enzyme