Any feedback?
Literature summary for 6.3.4.3 extracted from
- Impact of mutating the key residues of a bifunctional 5,10-methylenetetrahydrofolate dehydrogenase-cyclohydrolase from Escherichia coli on its activities (2015), Biochemistry, 54, 3504-3513 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium perfringens | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FHS | - |
Clostridium perfringens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in Escherichia coli, the essential function of folD can be replaced by Clostridium perfringens Fhs. The Fhs-supported folD deletion strains grow well in a complex medium and require purines and glycine as supplements for growth in M9 minimal medium. The in vivo levels of N10-formyltetrahydrofolate in the folD deletion strain carrying plasmid-borne Fhs are limiting. The folD deletion strain carrying harboring Fhs on the chromosome shows a high NADP+-to-NADPH ratio and hypersensitivity to trimethoprim | Clostridium perfringens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
