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0.002 - 0.021
(6S)-tetrahydrofolate
0.291 - 0.98
5,10-methylenetetrahydrofolate
57.86 - 61.95
DL-3-phenylserine
0.27 - 131.6
DL-phenylserine
0.003 - 3.4
tetrahydrofolate
0.1
tetrahydromethanopterin
-
pH 7.4, 37°C
additional information
additional information
-
0.002
(6S)-tetrahydrofolate
pH 7.2, 37°C
0.0052
(6S)-tetrahydrofolate
pH 7.0, 25°C, recombinant enzyme, with L-serine in HEPES buffer
0.007
(6S)-tetrahydrofolate
pH 7.0, 25°C, recombinant enzyme, with L-serine in phosphate buffer
0.021
(6S)-tetrahydrofolate
pH 7.0, 25°C, recombinant enzyme, with D-serine
0.291
5,10-methylenetetrahydrofolate
isoform SHMT1, at pH 8.8 and 30°C
0.98
5,10-methylenetetrahydrofolate
isoform SHMT2, at pH 8.8 and 30°C
0.071
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25°C
47
D-serine
-
apparent value, in 50 mM HEPES buffer (pH 7.0), at 25°C
55
D-serine
pH 7.0, 25°C, recombinant enzyme
57.86
DL-3-phenylserine
wild type enzyme, at pH 7.8 and 30°C
61.95
DL-3-phenylserine
mutant enzyme I249L, at pH 7.8 and 30°C
0.27
DL-phenylserine
-
wild type enzyme, at pH 7.0 and 37°C
81.9
DL-phenylserine
-
mutant enzyme G132P, at pH 7.0 and 37°C
93.2
DL-phenylserine
-
mutant enzyme H61G/G132P, at pH 7.0 and 37°C
131.6
DL-phenylserine
-
mutant enzyme H61G, at pH 7.0 and 37°C
0.556
glycine
isoform SHMT1, at pH 8.8 and 30°C
0.66
glycine
isoform SHMT2, at pH 8.8 and 30°C
0.68
glycine
-
pH 7.5, 70°C
0.13
L-Ser
-
mutant enzyme P218A
0.13
L-Ser
-
mutant enzyme P218G
0.14
L-Ser
-
mutant enzyme P214A
0.24
L-Ser
-
mutant enzyme P214G
0.25
L-Ser
-
mutant enzyme P216A
0.3
L-Ser
-
wild-type enzyme
0.33
L-Ser
-
mutant enzyme P264A
0.58
L-Ser
-
mutant enzyme P216G
0.8
L-Ser
recombinant wild-type enzyme
1
L-Ser
-
pH 7.4, 37°C, wild-type enzyme
1.3
L-Ser
-
pH 7.4, 37°C, mutant enzyme S52A
1.33
L-Ser
-
mutant enzyme P264G
4
L-Ser
mutant enzyme E75Q
5.2
L-Ser
-
pH 7.4, 37°C, mutant enzyme R262A
8
L-Ser
-
mutant enzyme P258A
11.2
L-Ser
-
pH 7.4, 37°C, mutant enzyme S52C
0.1
L-serine
apparent value, isoform SHMT1, at pH 7.2 and 20°C
0.1
L-serine
wild type enzyme SHMT1, at pH 7.2 and 20°C
0.11
L-serine
-
at pH 7.9, temperature not specified in the publication
0.12
L-serine
-
at pH 8.3, temperature not specified in the publication
0.14
L-serine
apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.15
L-serine
apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.15 - 0.9
L-serine
-
recombinant enzyme
0.15 - 0.9
L-serine
-
recombinant enzyme
0.15 - 0.9
L-serine
-
mutant enzyme Y82F
0.16
L-serine
-
at pH 8.3, temperature not specified in the publication
0.17
L-serine
pH 7.0, 25°C, recombinant enzyme, in phosphate buffer
0.18
L-serine
-
in 50 mM HEPES buffer (pH 7.0), at 25°C
0.18
L-serine
pH 7.0, 25°C, recombinant enzyme, in HEPES buffer
0.18
L-serine
-
at pH 7.9, temperature not specified in the publication
0.2
L-serine
pH 7.2, 37°C
0.2
L-serine
apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
-
at pH 7.5, temperature not specified in the publication
0.22
L-serine
-
at pH 7.5, temperature not specified in the publication
0.23
L-serine
-
at pH 7.1, temperature not specified in the publication
0.251
L-serine
-
in phosphate buffer, pH 7.45, at 25°C
0.278
L-serine
apparent value, isoform SHMT2, at pH 7.2 and 20°C
0.28
L-serine
-
pH 7.5, 70°C
0.28
L-serine
-
at pH 7.1, temperature not specified in the publication
0.29
L-serine
pH and temperature not specified in the publication
0.3
L-serine
pH 7.2, 20°C
0.3
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
0.3
L-serine
-
at pH 6.6, temperature not specified in the publication
0.31
L-serine
-
pH and temperature not specified in the publication
0.314
L-serine
mutant H135N/R137A/E168N, at pH 7.2 and 20°C
0.371
L-serine
-
in 50 mM HEPES buffer, pH 7.45, at 25°C
0.4
L-serine
pH 7.2, 20°C
0.42
L-serine
-
at pH 6.6, temperature not specified in the publication
0.45
L-serine
isoform SHMT2, at pH 7.8 and 30°C
0.57
L-serine
mutant H135N/R137A, at pH 7.2 and 20°C
0.7
L-serine
-
only tetrameric form
0.7
L-serine
-
in 50 mM Tris-HCl pH 8.0, at 37°C
0.9
L-serine
-
only dimeric form
0.9
L-serine
wild type enzyme, at 37°C
1
L-serine
-
mitochondrial enzyme
1
L-serine
-
recombinant enzyme
1
L-serine
mutant enzyme F315G, at 37°C
1.3
L-serine
-
cytosolic enzyme
1.5
L-serine
-
mutant enzyme E74Q
1.8
L-serine
-
wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C
2.2
L-serine
isoform SHMT2, at pH 7.2 and 30°C
3.3
L-serine
-
mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C
4
L-serine
-
mutant enzyme
4.2
L-serine
-
mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C
4.8
L-serine
isoform SHMT1, at pH 7.2 and 30°C
0.43
serine
-
0.003
tetrahydrofolate
-
mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C
0.0031
tetrahydrofolate
-
mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C
0.0037
tetrahydrofolate
-
mutant L474F
0.0041
tetrahydrofolate
-
wild-type
0.00435
tetrahydrofolate
apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.005
tetrahydrofolate
-
at pH 6.6, temperature not specified in the publication
0.00703
tetrahydrofolate
apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.00716
tetrahydrofolate
apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.009
tetrahydrofolate
mutant L474F
0.01
tetrahydrofolate
wild-type
0.01
tetrahydrofolate
-
mutant S394N
0.011
tetrahydrofolate
-
at pH 7.1, temperature not specified in the publication
0.0112
tetrahydrofolate
apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.014
tetrahydrofolate
-
mutant enzyme H132A, in the presence of NADP+, at pH 3.0 and 30°C
0.015
tetrahydrofolate
-
wild-type enzyme
0.017
tetrahydrofolate
-
mutant enzyme P218G
0.017
tetrahydrofolate
-
mutant enzyme P264A
0.018
tetrahydrofolate
-
at pH 7.5, temperature not specified in the publication
0.019
tetrahydrofolate
-
mutant enzyme P218A
0.02
tetrahydrofolate
-
recombinant enzyme
0.02
tetrahydrofolate
-
mutant enzyme P214A
0.02
tetrahydrofolate
-
mutant enzyme P214G
0.02
tetrahydrofolate
-
mutant enzyme P216A
0.02
tetrahydrofolate
apparent value, isoform SHMT1, at pH 7.2 and 20°C
0.023
tetrahydrofolate
apparent value, isoform SHMT2, at pH 7.2 and 20°C
0.025
tetrahydrofolate
mutant S394N
0.032
tetrahydrofolate
isoform SHMT2, at pH 7.8 and 30°C
0.033
tetrahydrofolate
isoform SHMT1, at pH 7.2 and 30°C
0.038
tetrahydrofolate
-
at pH 8.3, temperature not specified in the publication
0.04 - 0.046
tetrahydrofolate
-
-
0.04 - 0.046
tetrahydrofolate
-
recombinant enzyme
0.04 - 0.046
tetrahydrofolate
-
glycine
0.042
tetrahydrofolate
-
at pH 7.9, temperature not specified in the publication
0.048
tetrahydrofolate
-
at pH 7.1, temperature not specified in the publication
0.049
tetrahydrofolate
-
at pH 7.9, temperature not specified in the publication
0.051
tetrahydrofolate
-
at pH 6.6, temperature not specified in the publication
0.054
tetrahydrofolate
-
at pH 7.5, temperature not specified in the publication
0.055
tetrahydrofolate
-
wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C
0.065
tetrahydrofolate
-
pH and temperature not specified in the publication
0.08
tetrahydrofolate
-
-
0.085
tetrahydrofolate
-
mutant enzyme P216G
0.086
tetrahydrofolate
pH and temperature not specified in the publication
0.094
tetrahydrofolate
-
at pH 8.3, temperature not specified in the publication
0.14
tetrahydrofolate
-
in 50 mM HEPES buffer (pH 7.0), at 25°C
0.193
tetrahydrofolate
-
in 50 mM HEPES buffer, pH 7.45, at 25°C
0.2177
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
0.223
tetrahydrofolate
isoform SHMT2, at pH 7.2 and 30°C
0.25
tetrahydrofolate
-
-
0.253
tetrahydrofolate
-
in phosphate buffer, at 25°C
0.3
tetrahydrofolate
-
mutant K251R, without pyridoxal phosphate
0.82
tetrahydrofolate
-
recombinant enzyme
0.89
tetrahydrofolate
-
wild-type, in the presence of 0.25 mM pyridoxal phosphate
1
tetrahydrofolate
-
wild-type, without pyridoxal phosphate
1.16
tetrahydrofolate
-
mutant K251R, in the presence of 0.25 mM pyridoxal phosphate
2.1
tetrahydrofolate
-
mutant enzyme
3.4
tetrahydrofolate
-
in 50 mM Tris-HCl pH 8.0, at 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
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pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
allosteric kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
kinetic analysis of ternary complex mechanism, determination of ligand binding, transient, single-turnover and bi-substrate steady-state kinetics, detailed overview. The enzyme can bind first to either L-serine or tetrahydrofolate. The dissociation constants for the enzyme-L-serine and enzyme-tetrahydrofolate complexes are 0.18 mM and 0.35 mM, respectively. The kinetic mechanism of PvSHMT occurs via a random-order model and glycine formation is the rate-limiting step of the enzyme reaction
-