EC Number |
Application |
Reference |
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6.3.3.2 | 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 |
715571 |
6.3.3.2 | 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 |
745499 |
6.3.3.2 | medicine |
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 |
662472 |
6.3.3.2 | pharmacology |
the enzyme could be a potentially important enzyme as a target in chemotherapy |
1325 |