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
-
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
- 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
ECTree
Advanced search results
Application
Application on EC 6.3.3.2 - 5-formyltetrahydrofolate cyclo-ligase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
analysis
development of a functional complementation assay for 5-CHO-THF metabolism in Escherichia coli, based on deleting the gene encoding 5-FCL. The deletion mutant accumulates 5-formyltetrahydrofolate and,with glycine as sole nitrogen source, shows a growth defect, both phenotypes are complemented by bacterial or archaeal genes encoding glutamate formiminotransferase. Glutamate formiminotransferases functionally replace 5-formyltetrahydrofolate cyclo-ligases in certain prokaryotes
medicine
pharmacology
-
the enzyme could be a potentially important enzyme as a target in chemotherapy
-
the enzyme is important in cancer treatment to rescue cells from high dose levels of the anti-folate methotrexate, and to potentiate the antitumor activity of 5-fluorouracil
medicine
identification of four patients from two different families, due to a missense mutation (c.806C>T, p.Thr296Ile) and a splice site mutation (c.1674G>A) leading to exon skipping,while the other three patients harboured a missense mutation (c.146C>T, p.Ser49Phe) and a premature stop mutation (c.673G>T, p.Glu225*). Patient fibroblasts show severely reduced methionine formation from [14C]-formate, which does not increase in cobalamin supplemented culture medium but is responsive to folic and folinic acid