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Literature summary for 6.3.4.3 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 fhs, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Rosetta | Clostridium perfringens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens gene fhs. Simultaneous presence of Clostridium perfringens 5,10-methenyltetrahydrofolate dehydrogenase and 5,10-methenyltetrahydrofolate cyclohydrolase, CpeFolD and CpeFchA, supports the growth of the DELTAfolD/pCpeFhs strain in M9 minimal medium, and rescues it for its requirements for formate and glycine | Clostridium perfringens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.091 | - |
ATP | pH 8.2, temperature not specified in the publication | Clostridium perfringens |  |
| 0.091 | - |
ATP | recombinant His6-tagged enzyme, pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
| 0.33 | - |
(6R,S)-tetrahydrofolate | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
| 0.33 | - |
(6R,S)-5,6,7,8-tetrahydrofolate | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
| 0.33 | - |
(6R,S)-tetrahydrofolate | recombinant His6-tagged enzyme, pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
| 3 | - |
formate | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
| 3 | - |
formate | recombinant His6-tagged enzyme, pH 8.2, 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. |
|---|---|---|---|---|---|---|
| ATP + formate + tetrahydrofolate | Clostridium perfringens | - |
ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
| ATP + formate + tetrahydrofolate | Clostridium perfringens DSM 756 | - |
ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium perfringens | - |
- |
- |
| Clostridium perfringens | Q0TMI3 | - |
- |
| Clostridium perfringens DSM 756 | Q0TMI3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Clostridium perfringens |
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS Rosetta by nickel affinity chromatography | Clostridium perfringens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + formate + (6R,S)-5,6,7,8-tetrahydrofolate | - |
Clostridium perfringens | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
| ATP + formate + (6R,S)-5,6,7,8-tetrahydrofolate | - |
Clostridium perfringens DSM 756 | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
| ATP + formate + (6R,S)-tetrahydrofolate | - |
Clostridium perfringens | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
| ATP + formate + (6R,S)-tetrahydrofolate | - |
Clostridium perfringens DSM 756 | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
| ATP + formate + tetrahydrofolate | - |
Clostridium perfringens | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
| ATP + formate + tetrahydrofolate | - |
Clostridium perfringens DSM 756 | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CpeFhs | - |
Clostridium perfringens |
| FHS | - |
Clostridium perfringens |
| Formyltetrahydrofolate synthetase | - |
Clostridium perfringens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.2 | - |
assay at | Clostridium perfringens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Clostridium perfringens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | most organisms possess bifunctional FolD [5,10-methylenetetrahydrofolate (5,10-CH2-THF) dehydrogenase-cyclohydrolase] to generate NADPH and 10-formyltetrahdrofolate (10-CHO-THF) required in various metabolic steps. In addition, some organisms including Clostridium perfringens possess another protein, Fhs (formyltetrahydrofolate synthetase), to synthesize 10-CHO-THF. The presence of the three clostridial proteins, monofunctional 5,10-methenyltetrahydrofolate dehydrogenase FolD, 5,10-methenyltetrahydrofolate cyclohydrolase FchA, and 10-formyltetrahdrofolate synthetase Fhs, is required to maintain folate homeostasis in the cell, overview | Clostridium perfringens |
| metabolism | the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials | Clostridium perfringens |
| physiological function | expression of Clostridium perfringens Fhs and FolD-FchA rescue the photosensitive phenotype of an Escherichia coli DELTAGlyA strain | Clostridium perfringens |
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