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araATP + 5-formyltetrahydrofolate
araADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
ATP + (6R,S)-5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + (6R,S)-5-formyltetrahydropteroyl-Glu
?
-
-
-
-
?
ATP + (6S)-5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
ATP + (6S)-5-formyltetrahydropteroyl-pentaglutamate
?
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
ATP + 5-formyltetrahydrofolate-pentaglutamate
ADP + phosphate + 5,10-methylenetetrahydrofolate-pentaglutamate
preferred substrate to the monoglutamyl form
-
ir
ATP + 5-formyltetrahydrohomofolate
?
-
-
-
-
?
ATP + 5-formyltetrahydropteroyl-pentaglutamate
?
ATPgammaS + 5-formyltetrahydrofolate
ADPgammaS + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
CTP + 5-formyltetrahydrofolate
CDP + phosphate + 5,10-methenyltetrahydrofolate
-
CTP in form of MgCTP2-
-
-
?
CTP + 5-formyltetrahydrofolate
CDP + phosphate + 5,10-methylenetetrahydrofolate
dATP + 5-formyltetrahydrofolate
dADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
dTTP + 5-formyltetrahydrofolate
dTDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
GTP + 5-formyltetrahydrofolate
GDP + phosphate + 5,10-methylenetetrahydrofolate
ITP + 5-formyltetrahydrofolate
IDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
UTP + 5-formyltetrahydrofolate
UDP + phosphate + 5,10-methenyltetrahydrofolate
-
UTP in form of MgUTP2-
-
-
?
UTP + 5-formyltetrahydrofolate
UDP + phosphate + 5,10-methylenetetrahydrofolate
additional information
?
-
ATP + (6S)-5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
?
ATP + (6S)-5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
obligatory initial metabolic step in the intracellular conversion of 5-formyltetrahydrofolate to other reduced folates
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
it is proposed that methenyltetrahydrofolate synthetase is a salvage enzyme which converts the nonenzymatically formed and nonmetabolically active 5-formyltetrahydropteroyl-(Glu)n back into the one-carbon donor folate pool. It is also possible that methenyltetrahydrofolate synthetase is part of a regulation system in the cell in which its substrate 5-formyl-tetrahydropteroyl-(Glu)n plays a role as a regulator of one-carbon metabolism by inhibiting other folate requiring enzymes
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
key enzymatic reaction in the pathway by which 5-formyltetrahydrofolate enters the folate coenzyme pool
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
recycling reaction
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
Q81LX0
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
Q81LX0
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
important reaction in one-carbon donor recycling
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
i.e. 5-FTHF or leucovirin
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
the enzyme affects intracellular folate concentrations by accelerating folate degradation
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
the enzyme affects intracellular folate concentrations by accelerating folate degradation
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
enzyme prefers the polyglutamate forms of the substrate compared to the monoglutamate form
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
enzyme plays an important role in one-carbon metabolism, overview about folate catabolism
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
folate binds in a spherical pocket, substrate binding and active site structure, structure-function analysis, detailed overview
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
ATP in form of MgATP2-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
ATP in form of MgATP2-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
ATP in form of MgATP2-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
ATP in form of MgATP2-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
enzyme plays a central role in the regulation of folate-dependent, one-carbon metabolism
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
ATP in form of MgATP2-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?, ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
no reverse reaction detected
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
(6R,S)-5-formyltetrahydrofolate, (6S)-5-formyltetrahydrofolate
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
i.e. leucovorin, ir
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
i.e. leucovorin, ir
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydropteroyl-pentaglutamate
?
-
-
-
-
?
ATP + 5-formyltetrahydropteroyl-pentaglutamate
?
-
-
-
-
?
CTP + 5-formyltetrahydrofolate
CDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
CTP + 5-formyltetrahydrofolate
CDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
CTP + 5-formyltetrahydrofolate
CDP + phosphate + 5,10-methylenetetrahydrofolate
-
as effective as ATP
-
-
?
GTP + 5-formyltetrahydrofolate
GDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
GTP + 5-formyltetrahydrofolate
GDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
UTP + 5-formyltetrahydrofolate
UDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
UTP + 5-formyltetrahydrofolate
UDP + phosphate + 5,10-methylenetetrahydrofolate
-
-
-
-
?
additional information
?
-
enzyme is specific for the 6S-isomer
-
?
additional information
?
-
-
increased MTHFS expression affects the efficacy of the glycinamide ribonucleotide formyltransferase inhibitor LY309887, overview. SH-SY5Y neuroblastoma with increased MTHFS expression display a 4fold resistance to the GARFT inhibitor LY309887, but do not exhibit resistance to the thymidylate synthase inhibitor Pemetrexed.
-
-
?
additional information
?
-
disruption of folate metabolism is associated with several pathologies and developmental anomalies including cancer and neural tube defects
-
-
?
additional information
?
-
-
disruption of folate metabolism is associated with several pathologies and developmental anomalies including cancer and neural tube defects
-
-
?
additional information
?
-
-
5-formyltetrahydrohomofolate, 10-formyltetrahydrohomofolate, and 5-formyl,10-methyltetrahydrofolate are no substrates
-
-
?
additional information
?
-
disruption of folate metabolism is associated with several pathologies and developmental anomalies including cancer and neural tube defects
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 5-formyltetrahydrofolate
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
additional information
?
-
ATP + 5-formyltetrahydrofolate
?
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
obligatory initial metabolic step in the intracellular conversion of 5-formyltetrahydrofolate to other reduced folates
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
it is proposed that methenyltetrahydrofolate synthetase is a salvage enzyme which converts the nonenzymatically formed and nonmetabolically active 5-formyltetrahydropteroyl-(Glu)n back into the one-carbon donor folate pool. It is also possible that methenyltetrahydrofolate synthetase is part of a regulation system in the cell in which its substrate 5-formyl-tetrahydropteroyl-(Glu)n plays a role as a regulator of one-carbon metabolism by inhibiting other folate requiring enzymes
-
-
?
ATP + 5-formyltetrahydrofolate
?
-
key enzymatic reaction in the pathway by which 5-formyltetrahydrofolate enters the folate coenzyme pool
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
recycling reaction
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
important reaction in one-carbon donor recycling
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
the enzyme affects intracellular folate concentrations by accelerating folate degradation
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
the enzyme affects intracellular folate concentrations by accelerating folate degradation
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
enzyme plays an important role in one-carbon metabolism, overview about folate catabolism
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
enzyme plays a central role in the regulation of folate-dependent, one-carbon metabolism
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
-
?
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
-
-
ir
additional information
?
-
-
increased MTHFS expression affects the efficacy of the glycinamide ribonucleotide formyltransferase inhibitor LY309887, overview. SH-SY5Y neuroblastoma with increased MTHFS expression display a 4fold resistance to the GARFT inhibitor LY309887, but do not exhibit resistance to the thymidylate synthase inhibitor Pemetrexed.
-
-
?
additional information
?
-
disruption of folate metabolism is associated with several pathologies and developmental anomalies including cancer and neural tube defects
-
-
?
additional information
?
-
-
disruption of folate metabolism is associated with several pathologies and developmental anomalies including cancer and neural tube defects
-
-
?
additional information
?
-
disruption of folate metabolism is associated with several pathologies and developmental anomalies including cancer and neural tube defects
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.004
(6R,S)-5-formyltetrahydrofolate
-
-
0.0044 - 0.0047
(6R,S)-5-formyltetrahydropteroyl-Glu
0.002 - 0.005
(6S)-5-formyltetrahydrofolate
0.0008
(6S)-5-formyltetrahydropteroyl pentaglutamate
-
mitochondrial enzyme
0.0006
(6S)-5-formyltetrahydropteroyl-pentaglutamate
0.0002
5-formyl-tetrahydropteroyl-pentaglutamate
-
-
0.0005 - 130
5-formyltetrahydrofolate
additional information
additional information
-
0.0044
(6R,S)-5-formyltetrahydropteroyl-Glu
-
cytosolic enzyme
0.0047
(6R,S)-5-formyltetrahydropteroyl-Glu
-
-
0.0047
(6R,S)-5-formyltetrahydropteroyl-Glu
-
mitochondrial enzyme
0.002
(6S)-5-formyltetrahydrofolate
-
-
0.005
(6S)-5-formyltetrahydrofolate
pH 6.0, 28°C, recombinant enzyme
0.0006
(6S)-5-formyltetrahydropteroyl-pentaglutamate
-
-
0.0006
(6S)-5-formyltetrahydropteroyl-pentaglutamate
-
cytosolic enzyme
0.0005
5-formyltetrahydrofolate
-
-
0.0006
5-formyltetrahydrofolate
-
-
0.0025
5-formyltetrahydrofolate
wild type enzyme, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
0.0051
5-formyltetrahydrofolate
-
-
0.0071
5-formyltetrahydrofolate
mutant enzyme K120A, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
0.008
5-formyltetrahydrofolate
-
-
0.009
5-formyltetrahydrofolate
-
mutant enzyme Y151A, in 100 mM MES, pH 6.0, at 37°C
0.01
5-formyltetrahydrofolate
-
wild type enzyme, in 100 mM MES, pH 6.0, at 37°C
0.033
5-formyltetrahydrofolate
-
recombinant enzyme, pH 7.0, 30°C
0.047
5-formyltetrahydrofolate
-
mutant enzyme Y152F, in 100 mM MES, pH 6.0, at 37°C
0.14
5-formyltetrahydrofolate
-
-
0.165
5-formyltetrahydrofolate
-
pH 6.0, 37°C, recombinant enzyme
1 - 4
5-formyltetrahydrofolate
-
mutant enzyme D151A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
2.5
5-formyltetrahydrofolate
-
wild type enzyme, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
3
5-formyltetrahydrofolate
-
mutant enzyme Y152A, in 100 mM MES, pH 6.0, at 37°C
5.8
5-formyltetrahydrofolate
-
mutant enzyme D81A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
7.1
5-formyltetrahydrofolate
-
mutant enzyme K120A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
21
5-formyltetrahydrofolate
-
mutant enzyme W153A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
31
5-formyltetrahydrofolate
-
mutant enzyme R7A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
51
5-formyltetrahydrofolate
-
mutant enzyme K3A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
75
5-formyltetrahydrofolate
-
mutant enzyme R125A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
130
5-formyltetrahydrofolate
-
mutant enzyme K3D/D151K, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.0003
ATP
-
-
0.02
ATP
-
cytosolic enzyme
0.022
ATP
-
mitochondrial enzyme
0.043
ATP
-
recombinant enzyme, pH 7.0, 30°C
0.076
ATP
wild type enzyme, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
0.076
ATP
-
wild type enzyme, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.086
ATP
-
mutant enzyme D81A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.15
ATP
-
mutant enzyme D151A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.166
ATP
-
pH 6.0, 37°C, recombinant enzyme
0.3
ATP
-
Km-value is constant over the pH-range 5.0-7.5
0.769
ATP
recombinant enzyme
1.1
ATP
-
mutant enzyme K3D/D151K, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
1.2
ATP
mutant enzyme K120A, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
1.2
ATP
-
mutant enzyme K120A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
5
ATP
-
mutant enzyme K3A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
5
ATP
-
mutant enzyme R125A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
5
ATP
-
mutant enzyme R7A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
5
ATP
-
mutant enzyme W153A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.0016
CTP
-
-
0.0064
UTP
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
steady-state kinetics, recombinant enzyme
-
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16.3
(6S)-5-formyltetrahydrofolate
pH 6.0, 28°C, recombinant enzyme
0.02 - 5.3
5-formyltetrahydrofolate
additional information
additional information
-
0.02
5-formyltetrahydrofolate
-
mutant enzyme Y152A, in 100 mM MES, pH 6.0, at 37°C
0.046
5-formyltetrahydrofolate
-
mutant enzyme R7A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.1
5-formyltetrahydrofolate
-
mutant enzyme K3D/D151K, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.17
5-formyltetrahydrofolate
-
mutant enzyme K3A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.35
5-formyltetrahydrofolate
-
mutant enzyme R125A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.77
5-formyltetrahydrofolate
-
mutant enzyme D81A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.79
5-formyltetrahydrofolate
wild type enzyme, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
0.8
5-formyltetrahydrofolate
-
mutant enzyme W153A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
0.92
5-formyltetrahydrofolate
-
mutant enzyme Y151A, in 100 mM MES, pH 6.0, at 37°C
0.94
5-formyltetrahydrofolate
-
pH 6.0, 37°C, recombinant enzyme
1
5-formyltetrahydrofolate
-
wild type enzyme, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
1.3
5-formyltetrahydrofolate
mutant enzyme K120A, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
1.3
5-formyltetrahydrofolate
-
mutant enzyme D151A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
1.7
5-formyltetrahydrofolate
-
mutant enzyme K120A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C
3.33
5-formyltetrahydrofolate
-
wild type enzyme, in 100 mM MES, pH 6.0, at 37°C
4.3
5-formyltetrahydrofolate
-
mutant enzyme Y152F, in 100 mM MES, pH 6.0, at 37°C
5.3
5-formyltetrahydrofolate
truncated recombinant enzyme, pH 6.0, 23°C
0.99
ATP
-
pH 6.0, 37°C, recombinant enzyme
1
ATP
wild type enzyme, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
1.7
ATP
mutant enzyme K120A, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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D154A
site-directed mutagenesis, the mutant shows 0.9% of the wild-type catalytic activity
E225Stop
mutation identified in a patient suffering MTHFD1 deficiency
E61A
site-directed mutagenesis, the mutant shows 8.6% of the wild-type catalytic activity
F55A
site-directed mutagenesis, the mutant shows 53.6% of the wild-type catalytic activity
F85A
site-directed mutagenesis, the mutant shows 72.3% of the wild-type catalytic activity
K10A
site-directed mutagenesis, the mutant shows 7.5% of the wild-type catalytic activity
K150A
site-directed mutagenesis, the mutant shows wild-type catalytic activity
M58A
site-directed mutagenesis, the mutant shows 121.6% of the wild-type catalytic activity
M90A
site-directed mutagenesis, the mutant shows 49.2% of the wild-type catalytic activity
R145A
site-directed mutagenesis, the mutant shows 2.3% of the wild-type catalytic activity
R148A
site-directed mutagenesis, the mutant shows 30.7% of the wild-type catalytic activity
R14A
site-directed mutagenesis, the mutant shows 12.9% of the wild-type catalytic activity
S49F
mutation identified in a patient suffering MTHFD1 deficiency
T296I
mutation identified in a patient suffering MTHFD1 deficiency
W109A
site-directed mutagenesis, the mutant shows 39.7% of the wild-type catalytic activity
Y152A
site-directed mutagenesis, the mutant shows 24.9% of the wild-type catalytic activity
Y153A
site-directed mutagenesis, the mutant shows 3.2% of the wild-type catalytic activity
Y83A
site-directed mutagenesis, the mutant shows wild-type catalytic activity
Y151
-
able to use 5-formyltetrahydrohomofolate as a substrate
Y152A
-
increased turnover rate compared to the wild type enzyme
Y152F
-
decreased turnover rate compared to the wild type enzyme
D151A
-
the mutant shows increased turnover number compared to the wild type enzyme
D81A
-
the mutant shows reduced turnover number compared to the wild type enzyme
K3A
-
the mutant shows strongly reduced turnover number compared to the wild type enzyme
K3D/D151K
-
the mutant shows strongly reduced turnover number compared to the wild type enzyme
R115A
the mutant shows no activity
R125A
-
the mutant shows reduced turnover number compared to the wild type enzyme
R7A
-
the mutant shows severely reduced turnover number compared to the wild type enzyme
W153A
-
the mutant shows reduced turnover number compared to the wild type enzyme
K120A
the mutant shows increased Km and turnover number values for ATP and 5-formyltetrahydrofolate compared to the wild type enzyme
K120A
-
the mutant shows increased turnover number compared to the wild type enzyme
additional information
-
insertional mutation of the gene encoding the enzyme, At5g13050 or 28D07, reduces the growth rate of the mutant plants by 20% and delayes flowering by 1 week, and leads to accumulation of 5-formyltetrahydrofolate and glycine in leaves under photorespiratory conditions, effect of 5-formyltetrahydrofolate feeding, overview
additional information
-
truncation mutant comprising residues 6-202 of the enzyme is fully active and soluble
additional information
splice site mutation (c.1674G>A) identified in a patient suffering MTHFD1 deficiency leads to exon skipping
additional information
-
splice site mutation (c.1674G>A) identified in a patient suffering MTHFD1 deficiency leads to exon skipping
additional information
-
disruption mutants do not evoke an altered phenotype
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Bertrand, R.; MacKenzie, R.E.; Jolivot, J.
Human liver methenyltetrahydrofolate synthetase: improved purification and increased affinity for folate polyglutamate substrates
Biochim. Biophys. Acta
911
154-161
1987
Homo sapiens
brenda
Huennekens, F.M.; Henderson, G.B.; Vitols, K.S.; Grimshaw, C.E.
Enzymatic activation of 5-formyltetrahydrofolate via conversion to 5,10-methenyltetrahydrofolate
Adv. Enzyme Regul.
22
3-13
1984
Gallus gallus, Oryctolagus cuniculus, Ovis aries, Lacticaseibacillus casei, Mus musculus
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Hopkins, S.; Schirch, V.
5,10-Methenyltetrahydrofolate synthetase. Purification and properties of the enzyme from rabbit liver
J. Biol. Chem.
259
5618-5622
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Oryctolagus cuniculus
brenda
Grimshaw, C.E.; Henderson, G.B.; Soppe, G.G.; Hansen, G.; Mathur, E.J.; Huennekens, F.M.
Purification and properties of 5,10-methenyltetrahydrofolate synthetase from Lactobacillus casei
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259
2728-2733
1984
Lacticaseibacillus casei
brenda
Greenberg, D.M.
N5-Formyltetrahydrofolic acid cyclodehydrase
Methods Enzymol.
18
786-789
1971
Ovis aries
-
brenda
Greenberg, D.M.; Wynston, L.K.; Nagabhushanam, A.
Further studies on N5-formyltetrahydrofolic acid cyclodehydrase
Biochemistry
4
1872-1878
1965
Ovis aries
-
brenda
Huang, T.; Schirch, V.
Mechanism for the coupling of ATP hydrolysis to the conversion of 5-formyltetrahydrofolate to 5,10-methenyltetrahydrofolate
J. Biol. Chem.
270
22296-22300
1995
Oryctolagus cuniculus
brenda
Dayan, A.; Bertrand, R.; Beauchemin, M.; Chahla, D.; Mamo, A.; Filion, M.; Skup, D.; Massie, B.; Jolivet, J.
Cloning and characterization of the human 5,10-methenyltetrahydrofolate synthetase-encoding cDNA
Gene
165
307-311
1995
Homo sapiens
brenda
Li, M.; Collier, C.; Gritsman, H.; Bertino, J.R.
Activity of 5,10-methenyltetrahydrofolate synthetase in rat tissues and in tumor cell lines
Pteridines
2
75-79
1990
Cricetulus griseus, Homo sapiens, Rattus norvegicus
-
brenda
Stover, P.; Huang, T.; Schirch, V.; Maras, B.; Valiante,S.; Barra, D.
Purification and properties of rabbit liver 5,10-methenyltetrahydrofolate synthetase
Chemistry and Biology of Pteridines and Folates (J. A. Ayling et al., eds., Plenum Press New York)
723-726
1993
Oryctolagus cuniculus
-
brenda
Jolivet, J.
Human 5,10-methenyltetrahydrofolate synthetase
Methods Enzymol.
281
162-170
1997
Homo sapiens
brenda
Bertrand, R.; Beauchemin, M.; Dayan, A.; Ouimet, M.; Jolivet, J.
Identification and characterization of human mitochondrial methenyltetrahydrofolate synthetase activity
Biochim. Biophys. Acta
1266
245-2549
1995
Homo sapiens
brenda
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Purification of folate-dependent enzymes from rabbit liver
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281
146-161
1997
Oryctolagus cuniculus
brenda
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18Oxygen incorporation into inorganic phosphate in the reaction catalyzed by N5,10-methenyltetrahydrofolate synthetase
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364
215-217
1995
Bos taurus
brenda
Thompson, H.R.; Jones, G.M.; Narkewicz, M.R.
Ontogeny of hepatic enzymes involved in serine- and folate-dependent one-carbon metabolism in rabbits
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280
G873-G878
2001
Oryctolagus cuniculus
brenda
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Cloning and characterization of methenyltetrahydrofolate synthetase from Saccharomyces cerevisiae
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277
20205-20213
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Saccharomyces cerevisiae
brenda
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Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants
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277
42748-42754
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Pisum sativum, Arabidopsis thaliana (Q8L539), Solanum lycopersicum (Q8LKF6), Solanum lycopersicum
brenda
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Methenyltetrahydrofolate synthetase regulates folate turnover and accumulation
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278
29856-29862
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Homo sapiens, Mus musculus
brenda
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5-Formyltetrahydrofolate is an inhibitory but well tolerated metabolite in Arabidopsis leaves
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280
26137-26142
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Arabidopsis thaliana
brenda
Copeland, E.H.; Ekiel, I.; Cygler, M.
Letter to the editor: 1H, 13C and 15N resonance assignments of human 5,10-methenyltetrahydrofolate synthetase
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29
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Homo sapiens
brenda
Anguera, M.C.; Liu, X.; Stover, P.J.
Cloning, expression, and purification of 5,10-methenyltetrahydrofolate synthetase from Mus musculus
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35
276-283
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Mus musculus (Q9D110), Mus musculus, Mus musculus 129/Sv (Q9D110)
brenda
Chen, S.; Shin, D.H.; Pufan, R.; Kim, R.; Kim, S.H.
Crystal structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI: 13508087) at 2.2.ANG. resolution
Proteins
56
839-843
2004
Mycoplasma pneumoniae
brenda
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Structural and functional characterization of a 5,10-methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI: 13508087)
Proteins
61
433-443
2005
Mycoplasma pneumoniae
brenda
Meier, C.; Carter, L.G.; Winter, G.; Owens, R.J.; Stuart, D.I.; Esnouf, R.M.
Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
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F63
168-172
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Methenyltetrahydrofolate synthetase is a high-affinity catecholamine-binding protein
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455
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2006
Oryctolagus cuniculus, Mus musculus
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Inhibition of 5,10-methenyltetrahydrofolate synthetase
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Mus musculus
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Field, M.S.; Szebenyi, D.M.; Stover, P.J.
Regulation of de novo purine biosynthesis by methenyltetrahydrofolate synthetase in neuroblastoma
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281
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Homo sapiens
brenda
Anantharaman, V.; Aravind, L.
Diversification of catalytic activities and ligand interactions in the protein fold shared by the sugar isomerases, eIF2B, DeoR transcription factors, acyl-CoA transferases and methenyltetrahydrofolate synthetase
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356
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Saccharomyces cerevisiae
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Investigations of the roles of arginine 115 and lysine 120 in the active site of 5,10-methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae
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27
303-308
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Mycoplasma pneumoniae (P75430), Mycoplasma pneumoniae
brenda
Field, M.; Anguera, M.; Page, R.; Stover, P.
5,10-Methenyltetrahydrofolate synthetase activity is increased in tumors and modifies the efficacy of antipurine LY309887
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481
145-150
2009
Homo sapiens, Mus musculus
brenda
Wu, D.; Li, Y.; Song, G.; Cheng, C.; Zhang, R.; Joachimiak, A.; Shaw, N.; Liu, Z.J.
Structural basis for the inhibition of human 5,10-methenyltetrahydrofolate synthetase by N10-substituted folate analogues
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69
7294-7301
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Homo sapiens (P49914), Homo sapiens
brenda
Jeanguenin, L.; Lara-Nunez, A.; Pribat, A.; Mageroy, M.H.; Gregory, J.F.; Rice, K.C.; de Crecy-Lagard, V.; Hanson, A.D.
Moonlighting glutamate formiminotransferases can functionally replace 5-formyltetrahydrofolate cycloligase
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285
41557-41566
2010
Escherichia coli (A0A061KWR9), Escherichia coli
brenda
Ogwang, S.; Nguyen, H.T.; Sherman, M.; Bajaksouzian, S.; Jacobs, M.R.; Boom, W.H.; Zhang, G.F.; Nguyen, L.
Bacterial conversion of folinic acid is required for antifolate resistance
J. Biol. Chem.
286
15377-15390
2011
Mycolicibacterium smegmatis (A0R3H2), Mycolicibacterium smegmatis
brenda
Tolley, M.; Bickford, L.; Clare, K.; Johann, T.W.
Investigations of amino acids in the ATP binding site of 5,10-methenyltetrahydrofolate synthetase
Protein J.
31
519-528
2012
Mycoplasma pneumoniae
brenda
Burda, P.; Kuster, A.; Hjalmarson, O.; Suormala, T.; Buerer, C.; Lutz, S.; Roussey, G.; Christa, L.; Asin-Cayuela, J.; Kollberg, G.; Andersson, B.A.; Watkins, D.; Rosenblatt, D.S.; Fowler, B.; Holme, E.; Froese, D.S.; Baumgartner, M.R.
Characterization and review of MTHFD1 deficiency four new patients, cellular delineation and response to folic and folinic acid treatment
J. Inherit. Metab. Dis.
38
863-872
2015
Homo sapiens (P11586), Homo sapiens
brenda