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0.85
2'-dAMP
-
cosubstrate ATP, pH 7.4, 27°C
0.73
7-deazaadenosine 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27°C
1.3 - 1.37
adenine-9-beta-D-arabinofuranoside 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27°C
additional information
additional information
-
0.006
2 ADP
-
cosubstrate ADP, pH 7.8, 25°C
-
0.006
2 ADP
-
ADP in form of MgADP-
-
0.088
2 ADP
-
ADP in form of MgADP-
-
0.15
2 ADP
-
cosubstrate AMP
-
0.15
2 ADP
-
ADP in form of MgADP-
-
0.15
2 ADP
-
ADP in form of MgADP-
-
0.003
ADP
-
cosubstrate MgADP-, pH 7.8, 25°C
0.046
ADP
-
25°C, pH 8.1, isoform N2
0.11
ADP
-
cosubstrate ATP, pH 8.5
0.128
ADP
Megalodesulfovibrio gigas
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.165
ADP
Megalodesulfovibrio gigas
Zn2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.23
ADP
pH 7.6, 16°C, recombinant enzyme
0.24 - 0.27
ADP
Rhodopseudomonas rubrum
-
-
0.24 - 0.27
ADP
-
25°C, pH 7.6
0.247
ADP
Megalodesulfovibrio gigas
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.28
ADP
nucleotide-binding domain 2 of wild type
0.3
ADP
nucleotide-binding domain 1 of wild type
0.32
ADP
pH 7.6, 16°C, enzyme from sperm flagellum
0.32
ADP
pH 7.6, isolated flagella
0.32
ADP
-
enzyme from sperm flagella, pH 7.6, 16°C
0.34 - 0.35
ADP
-
25°C, pH 8.0
0.34 - 0.35
ADP
-
cosubstrate ATP
0.34 - 0.35
ADP
-
pH 8.7, 25°C
0.45 - 0.55
ADP
-
30°C, pH 7.4
0.69
ADP
pH 7.6, 16°C, enzyme from embryonic cilia
0.69
ADP
-
enzyme from cilia, pH 7.6, 16°C
1.3
ADP
90°C, pH is not specified in the publication
2.2
ADP
in 100 mM TrisHCl (pH 7.5), 20 mM glucose, 5 mM MgCl2, 10 mM KCl, 2 mM dithiothreitol, at 37°C
0.03
ADP3-
-
pH 8, 25°C
0.09 - 0.092
ADP3-
-
pH 7.5, 30°C
0.09 - 0.092
ADP3-
-
25°C, pH 8.0
0.09 - 0.092
ADP3-
-
pH 8.7, 25°C
0.09 - 0.092
ADP3-
-
ATP production
0.09 - 0.092
ADP3-
-
ATP production
0.09 - 0.092
ADP3-
-
ADP, 30°C
0.0014
AMP
recombinant adenylate kinase 4, using GTP as cosubstrate
0.0053
AMP
recombinant adenylate kinase 4, using ATP as cosubstrate
0.00959
AMP
at 30°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.011
AMP
wild-type, pH 7.2, 27°C
0.013
AMP
mutant Q199R, pH 7.2, 27°C
0.016
AMP
wild-type, pH 7.2, 35°C
0.0214
AMP
at 22°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.0216
AMP
at 40°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.024
AMP
mutant Q199R, pH 7.2, 35°C
0.024
AMP
at 30°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.026
AMP
wild-type, pH 7.2, 45°C
0.037
AMP
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.0372
AMP
at 40°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.038 - 0.04
AMP
-
cosubstrate ATP, 30°C
0.038 - 0.04
AMP
-
pH 7.4, 27°C
0.038 - 0.04
AMP
-
pH 7.5, 25°C, ADP production
0.04
AMP
nucleotide-binding domain 2 of wild type
0.04
AMP
Megalodesulfovibrio gigas
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.046
AMP
mutant Q199R, pH 7.2, 45°C
0.046
AMP
Megalodesulfovibrio gigas
Zn2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.048
AMP
wild-type, pH 7.2, 55°C
0.048
AMP
-
in 50 mM Tris-HCl pH 7.6, 5 mM MgCl2, at 37°C
0.05
AMP
Q7Z0H0
pH 6.0 and pH 7.4
0.05547
AMP
at 60°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.06
AMP
nucleotide-binding domain 1 of wild type
0.069
AMP
-
cosubstrate MgATP, pH 7.8, 25°C
0.07
AMP
mutant G40R, 37°C, pH 8.0
0.07
AMP
mutant G40R, 37°C
0.07
AMP
wild-type, pH 7.2, 60°C
0.071
AMP
Megalodesulfovibrio gigas
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.07389
AMP
at 50°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.076 - 0.083
AMP
-
25°C, pH 8.0
0.08
AMP
mutant G64R, 37°C, pH 8.0
0.08
AMP
mutant G64R, 37°C
0.081
AMP
-
25°C, pH 8.1, isoform N1
0.094
AMP
mutant Q199R, pH 7.2, 55°C
0.11
AMP
mutant Q199R, pH 7.2, 60°C
0.114 - 0.13
AMP
-
pH 8.5
0.172
AMP
adenylate kinase 5 domain AK5p1, with ATP as phosphate donor
0.244
AMP
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.29
AMP
Q14EL6
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C
0.38
AMP
wild-type, 37°C, pH 8.0
0.5 - 0.6
AMP
-
cosubstrate ATP, 70°C
0.547
AMP
-
25°C, pH 8.1, isoform N2
1.01
AMP
mutant Y164C, 37°C, pH 8.0
1.01
AMP
mutant Y164C, 37°C
1.039
AMP
-
25°C, pH 8.1, isoform N1
1.1
AMP
90°C, pH is not specified in the publication
1.6
AMP
mutant R11128W, 37°C, pH 8.0
1.6
AMP
mutant R128W, 37°C
1.7
AMP
mutant D140del, 37°C, pH 8.0
1.7
AMP
mutant D140del, 37°C
0.000063
ATP
-
isoenzyme AK1, membrane protein fraction
0.000141
ATP
-
isoenzyme AK1b, cytosolic protein fraction
0.00073
ATP
-
isoenzyme AK1b, membrane protein fraction
0.000998
ATP
-
isoenzyme AK1, cytosolic protein fraction
0.0018
ATP
at 30°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 6 5mM KCl
0.002
ATP
at 22°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.002
ATP
at 40°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.00537
ATP
at 30°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.013
ATP
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.01659
ATP
at 40°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.025
ATP
-
cosubstrate AMP, pH 7.8, 25°C
0.025
ATP
-
ATP in form of MgATP2-
0.034
ATP
Megalodesulfovibrio gigas
Zn2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.036 - 0.037
ATP
-
ADP, 37°C
0.045
ATP
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.048 - 0.051
ATP
-
pH 7.4, 27°C
0.048 - 0.051
ATP
-
cosubstrate AMP, 30°C
0.049
ATP
Megalodesulfovibrio gigas
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.06
ATP
mutant G40R, 37°C, pH 8.0
0.06
ATP
mutant G40R, 37°C
0.06
ATP
-
ATP in form of MgATP2-
0.07
ATP
nucleotide-binding domain 2 of wild type
0.072
ATP
-
25°C, pH 8.1, isoform N2
0.072
ATP
-
ATP in form of MgATP2-
0.075
ATP
Q14EL6
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C
0.076
ATP
Megalodesulfovibrio gigas
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.08
ATP
nucleotide-binding domain 1 of wild type
0.084
ATP
-
cosubstrate 2'-dAMP, 27°C, pH 7.4
0.093
ATP
mutant enzyme CINAP H79G, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.09471
ATP
at 50°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.13
ATP
-
25°C, pH 8.1, isoform N1
0.13
ATP
wild-type, 37°C, pH 8.0
0.13
ATP
-
ATP in form of MgATP2-
0.1349
ATP
at 60°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.23
ATP
-
ATP in form of MgATP2-
0.27 - 0.3
ATP
-
25°C, pH 8.0
0.27 - 0.3
ATP
-
cosubstrate 3'-dAMP, pH 7.4, 27°C
0.272
ATP
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.38
ATP
mutant G64R, 37°C, pH 8.0
0.38
ATP
mutant G64R, 37°C
0.4
ATP
mutant D140del, 37°C, pH 8.0
0.4
ATP
mutant D140del, 37°C
0.5
ATP
mutant Y164C, 37°C, pH 8.0
0.5
ATP
mutant Y164C, 37°C
1.03
ATP
mutant R11128W, 37°C, pH 8.0
1.03
ATP
mutant R128W, 37°C
1.1
ATP
90°C, pH is not specified in the publication
0.507
dAMP
recombinant adenylate kinase 4, using ATP as cosubstrate
2
dAMP
Km above 2.0 mM, adenylate kinase 5 domain AK5p1, with ATP as phosphate donor
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10°C to 50°C. Identification of key residues and contacts responsible for the conformational transitions are identified by following the time evolution of the two-dimensional spatial contact maps and characterizing the transition state as well as intermediate structure ensembles
-