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Literature summary for 1.5.1.5 extracted from
- Physiological role of FolD (methylenetetrahydrofolate dehydrogenase), FchA (methenyltetrahydrofolate cyclohydrolase) and Fhs (formyltetrahydrofolate synthetase) from Clostridium perfringens in a heterologous model of Escherichia coli (2016), Microbiology, 162, 145-155 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli BL21 | Clostridium perfringens |
| gene folD, recombinant coexpression with Clostridium perfringens FchA in Escherichia coli strain K16 DELTA foldD mutants and functional complementation, overview | Clostridium perfringens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Clostridium perfringens | |
| 0.085 | - |
NADP+ | pH 7.6, temperature not specified in the publication | Clostridium perfringens |  |
| 0.228 | - |
5,10-methylenetetrahydrofolate | pH 7.6, temperature not specified in the publication | Clostridium perfringens | |
| 0.228 | - |
(6R,S)-5,10-methylenetetrahydrofolate | pH 7.6, temperature not specified in the publication | Clostridium perfringens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + NADP+ | Clostridium perfringens | - |
5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium perfringens | - |
- |
- |
| Clostridium perfringens | Q0TPD4 | monofunctional methylenetetrahydrofolate dehydrogenase. No methenyltetrahydrofolate cyclohydrolase activity | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Clostridium perfringens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (6R,S)-5,10-methylenetetrahydrofolate + NADP+ | monofunctional enzyme, no methenyltetrahydrofolate cyclohydrolase activity | Clostridium perfringens | 5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
| 5,10-methylenetetrahydrofolate + NADP+ | - |
Clostridium perfringens | 5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5,10-CH2-THF dehydrogenase | - |
Clostridium perfringens |
| 5,10-methylenetetrahydrofolate dehydrogenase | - |
Clostridium perfringens |
| Cpe FolD | - |
Clostridium perfringens |
| FolD | - |
Clostridium perfringens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Clostridium perfringens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Clostridium perfringens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the dehydrogenase activity of FolD catalyses NADP+-dependent oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate. The 5,10-methenyltetrahydrofolate cyclohydrolase activity in Clostridium perfringens is provided by another protein, the 5,10-methylenetetrahydrofolate cyclohydrolase FchA, whose cyclohydrolase activity is 10 times more efficient than that of Eco FolD. Both Clostridium perfringens FolD and FchA are required to substitute for the single bifunctional FolD in Escherichia coli. The simultaneous presence of Clostridium perfringens FolD and FchA is also necessary to rescue an Escherichia coli K16 folD deletion strain for its formate and glycine auxotrophies, and to alleviate its susceptibility to trimethoprim (an antifolate drug) or UV light | Clostridium perfringens |
| metabolism | the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials | Clostridium perfringens |
| physiological function | unlike the bifunctional enzyme FolD of Escherichia coli, and contrary to its annotated bifunctional nature, Clostridium perfringens FolD is a monofunctional 5,10-CH2-THF dehydrogenase. The dehydrogenase activity of Clostridium perfringens FolD is about five times more efficient than that of Escherichia coli FolD. FolD plays an important role in maintaining the NADP+/NADPH ratio | Clostridium perfringens |
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