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Literature summary for 2.7.1.28 extracted from

  • 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 (2014), J. Biol. Chem., 289, 10620-10636.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C404A the mutant shows reduced activity compared to the wild type enzyme Homo sapiens
H221A inactive Homo sapiens
K204A the mutant shows reduced activity compared to the wild type enzyme Homo sapiens
S446A the mutant shows reduced activity compared to the wild type enzyme Homo sapiens
T112A the mutant shows reduced activity compared to the wild type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00574
-
ATP mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0071
-
D-glyceraldehyde mutant enzyme S446A, at pH 7.5 and 37°C Homo sapiens
0.0099
-
dihydroxyacetone mutant enzyme S446A, at pH 7.5 and 37°C Homo sapiens
0.0137
-
D-glyceraldehyde mutant enzyme T112A, at pH 7.5 and 37°C Homo sapiens
0.015
-
D-glyceraldehyde mutant enzyme K204A, at pH 7.5 and 37°C Homo sapiens
0.0155
-
dihydroxyacetone wild type enzyme, at pH 7.5 and 37°C Homo sapiens
0.0162
-
D-glyceraldehyde mutant enzyme C404A, at pH 7.5 and 37°C Homo sapiens
0.0181
-
D-glyceraldehyde wild type enzyme, at pH 7.5 and 37°C Homo sapiens
0.0191
-
dihydroxyacetone mutant enzyme C404A, at pH 7.5 and 37°C Homo sapiens
0.0252
-
dihydroxyacetone mutant enzyme K204A, at pH 7.5 and 37°C Homo sapiens
0.0352
-
ATP mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0432
-
ATP wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0624
-
ATP wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0637
-
ATP mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0663
-
dihydroxyacetone mutant enzyme T112A, at pH 7.5 and 37°C Homo sapiens
0.0696
-
ATP mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0806
-
ATP mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0853
-
ATP mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.0996
-
ATP mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.183
-
ATP mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glyceraldehyde Homo sapiens
-
ADP + D-glyceraldehyde 3-phosphate
-
?
ATP + dihydroxyacetone Homo sapiens
-
ADP + dihydroxyacetone phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q3LXA3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glyceraldehyde
-
Homo sapiens ADP + D-glyceraldehyde 3-phosphate
-
?
ATP + dihydroxyacetone
-
Homo sapiens ADP + dihydroxyacetone phosphate
-
?
additional information no activity with glycolaldehyde and glycerol Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
homodimer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
dAK
-
Homo sapiens
dAK the gene encodes triokinase and FMN cyclase Homo sapiens
TKFC
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.13
-
dihydroxyacetone mutant enzyme S446A, at pH 7.5 and 37°C Homo sapiens
0.15
-
ATP mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.16
-
D-glyceraldehyde mutant enzyme T112A, at pH 7.5 and 37°C Homo sapiens
0.16
-
ATP mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.5
-
ATP mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.51
-
dihydroxyacetone mutant enzyme T112A, at pH 7.5 and 37°C Homo sapiens
0.66
-
ATP mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.74
-
D-glyceraldehyde mutant enzyme S446A, at pH 7.5 and 37°C Homo sapiens
1.7
-
ATP mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
2.09
-
D-glyceraldehyde mutant enzyme K204A, at pH 7.5 and 37°C Homo sapiens
2.1
-
ATP mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C Homo sapiens
2.17
-
ATP mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
2.26
-
dihydroxyacetone mutant enzyme C404A, at pH 7.5 and 37°C Homo sapiens
2.27
-
D-glyceraldehyde mutant enzyme C404A, at pH 7.5 and 37°C Homo sapiens
2.34
-
ATP mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
2.79
-
dihydroxyacetone mutant enzyme K204A, at pH 7.5 and 37°C Homo sapiens
3.94
-
ATP wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
4.59
-
ATP wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
4.83
-
D-glyceraldehyde wild type enzyme, at pH 7.5 and 37°C Homo sapiens
5
-
dihydroxyacetone wild type enzyme, at pH 7.5 and 37°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.19
-
ATP mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
0.64
-
ATP mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
1.15
-
ATP mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C Homo sapiens
1.2
-
D-glyceraldehyde mutant enzyme T112A, at pH 7.5 and 37°C Homo sapiens
1.9
-
ATP mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
2.18
-
ATP mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
2.4
-
ATP mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
2.6
-
ATP mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
4.2
-
ATP mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
6.3
-
ATP wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C Homo sapiens
7.6
-
dihydroxyacetone mutant enzyme T112A, at pH 7.5 and 37°C Homo sapiens
10.4
-
D-glyceraldehyde mutant enzyme S446A, at pH 7.5 and 37°C Homo sapiens
10.5
-
ATP wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C Homo sapiens
13.1
-
dihydroxyacetone mutant enzyme S446A, at pH 7.5 and 37°C Homo sapiens
14
-
D-glyceraldehyde mutant enzyme C404A, at pH 7.5 and 37°C Homo sapiens
14.2
-
D-glyceraldehyde mutant enzyme K204A, at pH 7.5 and 37°C Homo sapiens
27.5
-
D-glyceraldehyde wild type enzyme, at pH 7.5 and 37°C Homo sapiens
115
-
dihydroxyacetone mutant enzyme K204A, at pH 7.5 and 37°C Homo sapiens
118
-
dihydroxyacetone mutant enzyme C404A, at pH 7.5 and 37°C Homo sapiens
321
-
dihydroxyacetone wild type enzyme, at pH 7.5 and 37°C Homo sapiens