EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.5 | expression in Escherichia coli BL21 | Clostridium perfringens |
1.5.1.5 | gene folD, recombinant coexpression with Clostridium perfringens FchA in Escherichia coli strain K16 DELTA foldD mutants and functional complementation, overview | Clostridium perfringens |
3.5.4.9 | expression in Escherichia coli BL21 | Clostridium perfringens |
6.3.4.3 | expression in Escherichia coli BL21 | Clostridium perfringens |
6.3.4.3 | gene fhs, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Rosetta | Clostridium perfringens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.3.4.3 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.5 | additional information | - |
additional information | Michaelis-Menten kinetics | Clostridium perfringens | |
1.5.1.5 | 0.085 | - |
NADP+ | pH 7.6, temperature not specified in the publication | Clostridium perfringens | |
1.5.1.5 | 0.228 | - |
5,10-methylenetetrahydrofolate | pH 7.6, temperature not specified in the publication | Clostridium perfringens | |
1.5.1.5 | 0.228 | - |
(6R,S)-5,10-methylenetetrahydrofolate | pH 7.6, temperature not specified in the publication | Clostridium perfringens | |
3.5.4.9 | 0.157 | - |
(6R,S)-5,10-methenyltetrahydrofolate | pH 7.6, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 0.091 | - |
ATP | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 0.091 | - |
ATP | recombinant His6-tagged enzyme, pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 0.33 | - |
(6R,S)-tetrahydrofolate | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 0.33 | - |
(6R,S)-5,6,7,8-tetrahydrofolate | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 0.33 | - |
(6R,S)-tetrahydrofolate | recombinant His6-tagged enzyme, pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 3 | - |
formate | pH 8.2, temperature not specified in the publication | Clostridium perfringens | |
6.3.4.3 | 3 | - |
formate | recombinant His6-tagged enzyme, pH 8.2, temperature not specified in the publication | Clostridium perfringens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.5 | 5,10-methylenetetrahydrofolate + NADP+ | Clostridium perfringens | - |
5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
6.3.4.3 | ATP + formate + tetrahydrofolate | Clostridium perfringens | - |
ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + tetrahydrofolate | Clostridium perfringens DSM 756 | - |
ADP + phosphate + 10-formyltetrahydrofolate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.5 | Clostridium perfringens | - |
- |
- |
1.5.1.5 | Clostridium perfringens | Q0TPD4 | monofunctional methylenetetrahydrofolate dehydrogenase. No methenyltetrahydrofolate cyclohydrolase activity | - |
3.5.4.9 | Clostridium perfringens | A0A2X2Y2S3 | - |
- |
6.3.4.3 | Clostridium perfringens | - |
- |
- |
6.3.4.3 | Clostridium perfringens | Q0TMI3 | - |
- |
6.3.4.3 | Clostridium perfringens DSM 756 | Q0TMI3 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.1.5 | - |
Clostridium perfringens |
3.5.4.9 | - |
Clostridium perfringens |
6.3.4.3 | - |
Clostridium perfringens |
6.3.4.3 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS Rosetta by nickel affinity chromatography | Clostridium perfringens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.5 | (6R,S)-5,10-methylenetetrahydrofolate + NADP+ | monofunctional enzyme, no methenyltetrahydrofolate cyclohydrolase activity | Clostridium perfringens | 5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
1.5.1.5 | 5,10-methylenetetrahydrofolate + NADP+ | - |
Clostridium perfringens | 5,10-methenyltetrahydrofolate + NADPH + H+ | - |
? | |
3.5.4.9 | (6R,S)-5,10-methenyltetrahydrofolate + H2O | - |
Clostridium perfringens | 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + (6R,S)-5,6,7,8-tetrahydrofolate | - |
Clostridium perfringens | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + (6R,S)-5,6,7,8-tetrahydrofolate | - |
Clostridium perfringens DSM 756 | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + (6R,S)-tetrahydrofolate | - |
Clostridium perfringens | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + (6R,S)-tetrahydrofolate | - |
Clostridium perfringens DSM 756 | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + tetrahydrofolate | - |
Clostridium perfringens | ADP + phosphate + 10-formyltetrahydrofolate | - |
? | |
6.3.4.3 | ATP + formate + tetrahydrofolate | - |
Clostridium perfringens DSM 756 | ADP + phosphate + 10-formyltetrahydrofolate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.5 | 5,10-CH2-THF dehydrogenase | - |
Clostridium perfringens |
1.5.1.5 | 5,10-methylenetetrahydrofolate dehydrogenase | - |
Clostridium perfringens |
1.5.1.5 | Cpe FolD | - |
Clostridium perfringens |
1.5.1.5 | FolD | - |
Clostridium perfringens |
3.5.4.9 | 5,10-CH+-THF cyclohydrolase | - |
Clostridium perfringens |
3.5.4.9 | FchA | - |
Clostridium perfringens |
6.3.4.3 | CpeFhs | - |
Clostridium perfringens |
6.3.4.3 | FHS | - |
Clostridium perfringens |
6.3.4.3 | Formyltetrahydrofolate synthetase | - |
Clostridium perfringens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.1.5 | 7.6 | - |
assay at | Clostridium perfringens |
3.5.4.9 | 7.6 | - |
assay at | Clostridium perfringens |
6.3.4.3 | 8.2 | - |
assay at | Clostridium perfringens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.5 | NADP+ | - |
Clostridium perfringens | |
3.5.4.9 | NADP+ | - |
Clostridium perfringens | |
6.3.4.3 | ATP | - |
Clostridium perfringens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.5 | 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 |
1.5.1.5 | metabolism | the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials | Clostridium perfringens |
1.5.1.5 | 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 |
3.5.4.9 | metabolism | the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials | Clostridium perfringens |
6.3.4.3 | 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 |
6.3.4.3 | metabolism | the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials | Clostridium perfringens |
6.3.4.3 | physiological function | expression of Clostridium perfringens Fhs and FolD-FchA rescue the photosensitive phenotype of an Escherichia coli DELTAGlyA strain | Clostridium perfringens |