| Official Name |
|---|
| Dihydrofolate synthase.
|
| Alternative Name(s) |
|---|
| 7,8-dihydrofolate synthetase. |
| 7,8-dihydropteroate:L-glutamate ligase (ADP). |
| DHFS. |
| Dihydrofolate synthetase. |
| Dihydrofolate synthetase-folylpolyglutamate synthetase. |
| Dihydropteroate:L-glutamate ligase (ADP-forming). |
| FHFS. |
| FHFS/FPGS. |
| Folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase. |
| H(2)-folate synthetase. |
| Reaction catalysed |
|---|
| ATP + 7,8-dihydropteroate + L-glutamate <=> ADP + phosphate + 7,8-dihydropteroylglutamate |
| Comment(s) |
|---|
- In some bacteria, a single protein catalyzes both this activity and
that of EC 6.3.2.17, the combined activity of which leads to the
formation of the coenzyme polyglutamated tetrahydropteroate
(H(4)PteGlu(n)), i.e. various tetrahydrofolates.
- In contrast, the activities are located on separate proteins in most
eukaryotes studied to date.
- This enzyme is reponsible for attaching the first glutamate residue
to dihydropteroate to form dihydrofolate and is present only in those
organisms that have the ability to synthesize tetrahydrofolate de
novo, e.g. plants, most bacteria, fungi and protozoa.
|
| Cross-references |
|---|
| Biochemical Pathways; map number(s) | L2 |
| BRENDA | 6.3.2.12 |
| PUMA2 | 6.3.2.12 |
| PRIAM enzyme-specific profiles | 6.3.2.12 |
| KEGG Ligand Database for Enzyme Nomenclature | 6.3.2.12 |
| IUBMB Enzyme Nomenclature | 6.3.2.12 |
| IntEnz | 6.3.2.12 |
| MEDLINE | Find literature relating to 6.3.2.12 |
| MetaCyc | 6.3.2.12 |
| UniProtKB/Swiss-Prot |
|
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