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Literature summary extracted from

  • Aluri, S.; Sah, S.; Miryala, S.; Varshney, U.
    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 .
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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
-
?

Synonyms

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

pH Optimum

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

Cofactor

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

General Information

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