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Literature summary extracted from

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.5
-
Escherichia coli
3.5.4.9
-
Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.5 C58Y kcat/Km for 5,10-methenyltetrahydrofolate is 8.4fold lower than wild-type value Escherichia coli
1.5.1.5 D121A kcat/Km for 5,10-methenyltetrahydrofolate is 600fold lower than wild-type value Escherichia coli
1.5.1.5 G122D kcat/Km for 5,10-methenyltetrahydrofolate is 84fold lower than wild-type value Escherichia coli
1.5.1.5 K54S kcat/Km for 5,10-methenyltetrahydrofolate is identical to wild-type value Escherichia coli
1.5.1.5 Q98K very low activity with 5,10-methenyltetrahydrofolate Escherichia coli
1.5.1.5 R191E very low activity with 5,10-methenyltetrahydrofolate Escherichia coli
1.5.1.5 Y50S very low activity with 5,10-methenyltetrahydrofolate Escherichia coli
3.5.4.9 C58Y kcat/Km for 5,10-methenyltetrahydrofolate is 13.2fold lower than wild-type value Escherichia coli
3.5.4.9 D121A kcat/Km for 5,10-methenyltetrahydrofolate is 2348fold lower than wild-type value Escherichia coli
3.5.4.9 G122D kcat/Km for 5,10-methenyltetrahydrofolate is 283fold lower than wild-type value Escherichia coli
3.5.4.9 K54S very low activity with 5,10-methenyltetrahydrofolate Escherichia coli
3.5.4.9 Q98K very low activity with 5,10-methenyltetrahydrofolate Escherichia coli
3.5.4.9 R191E kcat/Km for 5,10-methenyltetrahydrofolate is 1.3fold higher than wild-type value Escherichia coli
3.5.4.9 Y50S very low activity with 5,10-methenyltetrahydrofolate Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.5 0.068
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme G122D Escherichia coli
1.5.1.5 0.104
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme D121A Escherichia coli
1.5.1.5 0.187
-
NADP+ pH 7.6, 30°C, wild-type enzyme Escherichia coli
1.5.1.5 0.205
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme K54S Escherichia coli
1.5.1.5 0.233
-
NADP+ pH 7.6, 30°C, mutant enzyme K54S Escherichia coli
1.5.1.5 0.279
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, wild-type enzyme Escherichia coli
1.5.1.5 0.302
-
NADP+ pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
1.5.1.5 0.302
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
3.5.4.9 0.0045
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme G122D Escherichia coli
3.5.4.9 0.015
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme D121A Escherichia coli
3.5.4.9 0.026
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, wild-type enzyme Escherichia coli
3.5.4.9 0.028
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme R191E Escherichia coli
3.5.4.9 0.04
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.9 5,10-methenyltetrahydrofolate + H2O Escherichia coli
-
10-formyltetrahydrofolate
-
?
3.5.4.9 5,10-methenyltetrahydrofolate + H2O Escherichia coli K12
-
10-formyltetrahydrofolate
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.5 Escherichia coli P24186
-
-
1.5.1.5 Escherichia coli K12 P24186
-
-
3.5.4.9 Escherichia coli P24186
-
-
3.5.4.9 Escherichia coli K12 P24186
-
-
6.3.4.3 Clostridium perfringens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.5
-
Escherichia coli
3.5.4.9
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.5 5,10-methylenetetrahydrofolate + NADP+
-
Escherichia coli 5,10-methenyltetrahydrofolate + NADPH + H+
-
?
1.5.1.5 5,10-methylenetetrahydrofolate + NADP+
-
Escherichia coli K12 5,10-methenyltetrahydrofolate + NADPH + H+
-
?
3.5.4.9 5,10-methenyltetrahydrofolate + H2O
-
Escherichia coli 10-formyltetrahydrofolate
-
?
3.5.4.9 5,10-methenyltetrahydrofolate + H2O
-
Escherichia coli K12 10-formyltetrahydrofolate
-
?

Synonyms

EC Number Synonyms Comment Organism
6.3.4.3 FHS
-
Clostridium perfringens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.9 30
-
assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.5 0.01
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme D121A Escherichia coli
1.5.1.5 0.06
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme G122D Escherichia coli
1.5.1.5 2.6
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
1.5.1.5 2.8
-
NADP+ pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
1.5.1.5 12.3
-
NADP+ pH 7.6, 30°C, mutant enzyme K54S Escherichia coli
1.5.1.5 14.3
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme K54S Escherichia coli
1.5.1.5 17.08
-
NADP+ pH 7.6, 30°C, wild-type enzyme Escherichia coli
1.5.1.5 19.9
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, wild-type enzyme Escherichia coli
3.5.4.9 0.01
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme D121A Escherichia coli
3.5.4.9 0.025
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme G122D Escherichia coli
3.5.4.9 4.75
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
3.5.4.9 40.9
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, wild-type enzyme Escherichia coli
3.5.4.9 57.4
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme R191E Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.9 7.6
-
assay at Escherichia coli

General Information

EC Number General Information Comment Organism
6.3.4.3 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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.1.5 0.096
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme D121A Escherichia coli
1.5.1.5 0.88
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme G122D Escherichia coli
1.5.1.5 8.6
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
1.5.1.5 9.2
-
NADP+ pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
1.5.1.5 52.7
-
NADP+ pH 7.6, 30°C, mutant enzyme K54S Escherichia coli
1.5.1.5 69.8
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme K54S Escherichia coli
1.5.1.5 71.3
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, wild-type enzyme Escherichia coli
1.5.1.5 91.3
-
NADP+ pH 7.6, 30°C, wild-type enzyme Escherichia coli
3.5.4.9 0.67
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme D121A Escherichia coli
3.5.4.9 5.55
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme G122D Escherichia coli
3.5.4.9 118.75
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme C58Y Escherichia coli
3.5.4.9 1573.1
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, wild-type enzyme Escherichia coli
3.5.4.9 2050
-
5,10-methenyltetrahydrofolate pH 7.6, 30°C, mutant enzyme R191E Escherichia coli