6.3.3.2: 5-formyltetrahydrofolate cyclo-ligase
This is an abbreviated version!
For detailed information about 5-formyltetrahydrofolate cyclo-ligase, go to the full flat file.
Word Map on EC 6.3.3.2
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6.3.3.2
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mthfr
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methylenetetrahydrofolate
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one-carbon
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homocysteine
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folate-dependent
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slc19a1
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10-formyltetrahydrofolate
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trifunctional
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cyclohydrolase
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5,10-methylenetetrahydrofolate
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remethylation
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folate-mediated
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folate-related
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1-carbon
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megaloblastic
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periconceptional
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folate-metabolizing
-
analysis
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pharmacology
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medicine
- 6.3.3.2
- mthfr
- methylenetetrahydrofolate
-
one-carbon
- homocysteine
-
folate-dependent
-
slc19a1
- 10-formyltetrahydrofolate
-
trifunctional
-
cyclohydrolase
- 5,10-methylenetetrahydrofolate
-
remethylation
-
folate-mediated
-
folate-related
-
1-carbon
-
megaloblastic
-
periconceptional
-
folate-metabolizing
- analysis
- pharmacology
- medicine
Reaction
Synonyms
5,10-methenyl-tetrahydrofolate synthetase, 5,10-Methenyltetrahydrofolate synthetase, 5,10-Methenyltetrahydropteroylglutamate synthetase, 5-CHO-THF cycloligase, 5-FCL, 5-Formyltetrahydrofolate cyclodehydrase, CH+-THF synthetase, Fau1p, Formyltetrahydrofolic cyclodehydrase, Methenyl THFS, Methenyl-THF synthetase, Methenyltetrahydrofolate synthetase, More, MTHFD1, MTHFS, N5-Formyltetrahydrofolic acid cyclodehydrase, Synthetase, methenyltetrahydrofolate, ygfA
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Metals Ions
Metals Ions on EC 6.3.3.2 - 5-formyltetrahydrofolate cyclo-ligase
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Ca2+
Co2+
Mg2+
Mn2+
additional information
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the enzyme is dependent on divalent cation, Mg2+ is preferred
Mg2+
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no divalent metal ion dependence beyond that required in the MgATP2- substrate complex
Mg2+
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dependent on, most effective divalent cation, required for MgATP2- complex formation, binding structure
Mg2+
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required in equivalent concentration with ATP, its only role is to form a complex with ATP