| 别名 |
100194131, AtDFB, cFPGS, DHFS/FPGS, dihydrofolate synthase/folylpolyglutamate synthase, eFPGS, Folate polyglutamate synthetase, FolC, folyl-gamma-glutamate synthetase, Folylpoly(.gamma.-glutamate) synthase, Folylpoly-.gamma.-glutamate synthase, Folylpoly-gamma-glutamate synthetase, Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase, Folylpolyglutamate synthase, Folylpolyglutamate synthetase, folylpolyglutamate synthetase 1, Folylpolyglutamyl synthetase, folypoly-gamma-glutamate synthetase, folypolyformyl glutamate synthase, folypolyglutamate synthase, folypolyglutamate synthetase, Formyltetrahydropteroyldiglutamate synthetase, FPGS, FPGS1, FPGS2, GRMZM2G393334, mFGPS, mFPGS, More, MTHFD1L, N10-Formyltetrahydropteroyldiglutamate synthetase, PfDHFS-FPGS, Synthetase, folylpolyglutamate, Tail length regulator, tetrahydrofolate:L-glutamate gamma-ligase (ADP-forming), tetrahydrofolylpolyglutamate synthase |
| Comments |
In some bacteria, a single protein catalyses both this activity and that of EC?6.3.2.12, dihydrofolate synthase [3], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates (H4folate). In contrast, the activities are located on separate proteins in most eukaryotes studied to date [4]. In?Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes [4]. As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C1?metabolism. (reviewed in [5]). The enzymes from different sources (particularly eukaryotes?versus?prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates. |
