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Literature summary for 1.5.1.3 extracted from

  • Yokota, A.; Takahashi, H.; Takenawa, T.; Arai, M.
    Probing the roles of conserved arginine-44 of Escherichia coli dihydrofolate reductase in its function and stability by systematic sequence perturbation analysis (2010), Biochem. Biophys. Res. Commun., 391, 1703-1707.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
R44A the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44C the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44D the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44E the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44F the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44G the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44I the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44K the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44L the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44M the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44N the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44P the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44Q the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44S the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44T the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44V the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44W the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli
R44Y the mutation significantly reduces the enzymatic activity and the binding affinity toward the cofactor NADPH Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0007
-
7,8-dihydrofolate mutant enzyme R44H, at 15°C, pH not specified in the publication Escherichia coli
0.0008
-
7,8-dihydrofolate mutant enzyme R44V, at 15°C, pH not specified in the publication Escherichia coli
0.001
-
7,8-dihydrofolate mutant enzyme R44Y, at 15°C, pH not specified in the publication Escherichia coli
0.0011
-
7,8-dihydrofolate mutant enzyme R44C, at 15°C, pH not specified in the publication Escherichia coli
0.0014
-
7,8-dihydrofolate mutant enzyme R44L, at 15°C, pH not specified in the publication Escherichia coli
0.0015
-
7,8-dihydrofolate mutant enzyme R44G, at 15°C, pH not specified in the publication Escherichia coli
0.0016
-
7,8-dihydrofolate mutant enzyme R44A, at 15°C, pH not specified in the publication Escherichia coli
0.0016
-
7,8-dihydrofolate wild type enzyme, at 15°C, pH not specified in the publication Escherichia coli
0.0019
-
7,8-dihydrofolate mutant enzyme R44E, at 15°C, pH not specified in the publication Escherichia coli
0.0021
-
7,8-dihydrofolate mutant enzyme R44I, at 15°C, pH not specified in the publication Escherichia coli
0.0023
-
7,8-dihydrofolate mutant enzyme R44M, at 15°C, pH not specified in the publication Escherichia coli
0.0024
-
7,8-dihydrofolate mutant enzyme R44Q, at 15°C, pH not specified in the publication Escherichia coli
0.0025
-
7,8-dihydrofolate mutant enzyme R44K, at 15°C, pH not specified in the publication Escherichia coli
0.0025
-
7,8-dihydrofolate mutant enzyme R44N, at 15°C, pH not specified in the publication Escherichia coli
0.0025
-
7,8-dihydrofolate mutant enzyme R44T, at 15°C, pH not specified in the publication Escherichia coli
0.0027
-
7,8-dihydrofolate mutant enzyme R44F, at 15°C, pH not specified in the publication Escherichia coli
0.0029
-
7,8-dihydrofolate mutant enzyme R44P, at 15°C, pH not specified in the publication Escherichia coli
0.003
-
7,8-dihydrofolate mutant enzyme R44D, at 15°C, pH not specified in the publication Escherichia coli
0.0031
-
7,8-dihydrofolate mutant enzyme R44S, at 15°C, pH not specified in the publication Escherichia coli
0.0037
-
7,8-dihydrofolate mutant enzyme R44W, at 15°C, pH not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydrofolate + NADPH + H+ Escherichia coli
-
5,6,7,8-tetrahydrofolate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrofolate + NADPH + H+
-
Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
?

Synonyms

Synonyms Comment Organism
DHFR
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.3
-
7,8-dihydrofolate mutant enzyme R44P, at 15°C, pH not specified in the publication Escherichia coli
0.69
-
7,8-dihydrofolate mutant enzyme R44D, at 15°C, pH not specified in the publication Escherichia coli
0.89
-
7,8-dihydrofolate mutant enzyme R44E, at 15°C, pH not specified in the publication Escherichia coli
0.89
-
7,8-dihydrofolate mutant enzyme R44Y, at 15°C, pH not specified in the publication Escherichia coli
0.98
-
7,8-dihydrofolate mutant enzyme R44L, at 15°C, pH not specified in the publication Escherichia coli
1.15
-
7,8-dihydrofolate mutant enzyme R44I, at 15°C, pH not specified in the publication Escherichia coli
1.31
-
7,8-dihydrofolate mutant enzyme R44V, at 15°C, pH not specified in the publication Escherichia coli
1.39
-
7,8-dihydrofolate mutant enzyme R44F, at 15°C, pH not specified in the publication Escherichia coli
1.59
-
7,8-dihydrofolate mutant enzyme R44H, at 15°C, pH not specified in the publication Escherichia coli
1.78
-
7,8-dihydrofolate mutant enzyme R44G, at 15°C, pH not specified in the publication Escherichia coli
1.9
-
7,8-dihydrofolate mutant enzyme R44Q, at 15°C, pH not specified in the publication Escherichia coli
2
-
7,8-dihydrofolate mutant enzyme R44T, at 15°C, pH not specified in the publication Escherichia coli
2.41
-
7,8-dihydrofolate mutant enzyme R44W, at 15°C, pH not specified in the publication Escherichia coli
2.43
-
7,8-dihydrofolate mutant enzyme R44C, at 15°C, pH not specified in the publication Escherichia coli
3.05
-
7,8-dihydrofolate mutant enzyme R44A, at 15°C, pH not specified in the publication Escherichia coli
3.3
-
7,8-dihydrofolate mutant enzyme R44N, at 15°C, pH not specified in the publication Escherichia coli
3.8
-
7,8-dihydrofolate mutant enzyme R44M, at 15°C, pH not specified in the publication Escherichia coli
5.4
-
7,8-dihydrofolate wild type enzyme, at 15°C, pH not specified in the publication Escherichia coli
5.7
-
7,8-dihydrofolate mutant enzyme R44K, at 15°C, pH not specified in the publication Escherichia coli
5.8
-
7,8-dihydrofolate mutant enzyme R44S, at 15°C, pH not specified in the publication Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
100
-
7,8-dihydrofolate mutant enzyme R44P, at 15°C, pH not specified in the publication Escherichia coli
230
-
7,8-dihydrofolate mutant enzyme R44D, at 15°C, pH not specified in the publication Escherichia coli
470
-
7,8-dihydrofolate mutant enzyme R44E, at 15°C, pH not specified in the publication Escherichia coli
500
-
7,8-dihydrofolate mutant enzyme R44F, at 15°C, pH not specified in the publication Escherichia coli
560
-
7,8-dihydrofolate mutant enzyme R44I, at 15°C, pH not specified in the publication Escherichia coli
660
-
7,8-dihydrofolate mutant enzyme R44W, at 15°C, pH not specified in the publication Escherichia coli
680
-
7,8-dihydrofolate mutant enzyme R44L, at 15°C, pH not specified in the publication Escherichia coli
800
-
7,8-dihydrofolate mutant enzyme R44Q, at 15°C, pH not specified in the publication Escherichia coli
800
-
7,8-dihydrofolate mutant enzyme R44T, at 15°C, pH not specified in the publication Escherichia coli
900
-
7,8-dihydrofolate mutant enzyme R44Y, at 15°C, pH not specified in the publication Escherichia coli
1200
-
7,8-dihydrofolate mutant enzyme R44G, at 15°C, pH not specified in the publication Escherichia coli
1300
-
7,8-dihydrofolate mutant enzyme R44N, at 15°C, pH not specified in the publication Escherichia coli
1600
-
7,8-dihydrofolate mutant enzyme R44M, at 15°C, pH not specified in the publication Escherichia coli
1700
-
7,8-dihydrofolate mutant enzyme R44V, at 15°C, pH not specified in the publication Escherichia coli
1900
-
7,8-dihydrofolate mutant enzyme R44A, at 15°C, pH not specified in the publication Escherichia coli
1900
-
7,8-dihydrofolate mutant enzyme R44S, at 15°C, pH not specified in the publication Escherichia coli
2200
-
7,8-dihydrofolate mutant enzyme R44C, at 15°C, pH not specified in the publication Escherichia coli
2300
-
7,8-dihydrofolate mutant enzyme R44K, at 15°C, pH not specified in the publication Escherichia coli
2500
-
7,8-dihydrofolate mutant enzyme R44H, at 15°C, pH not specified in the publication Escherichia coli
3400
-
7,8-dihydrofolate wild type enzyme, at 15°C, pH not specified in the publication Escherichia coli