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Literature summary 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)

EC Number Cloned (Comment) Organism
1.5.1.3 expressed in Escherichia coli JM109 cells Escherichia coli

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.3 0.0007
-
7,8-dihydrofolate mutant enzyme R44H, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0008
-
7,8-dihydrofolate mutant enzyme R44V, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.001
-
7,8-dihydrofolate mutant enzyme R44Y, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0011
-
7,8-dihydrofolate mutant enzyme R44C, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0014
-
7,8-dihydrofolate mutant enzyme R44L, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0015
-
7,8-dihydrofolate mutant enzyme R44G, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0016
-
7,8-dihydrofolate mutant enzyme R44A, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0016
-
7,8-dihydrofolate wild type enzyme, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0019
-
7,8-dihydrofolate mutant enzyme R44E, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0021
-
7,8-dihydrofolate mutant enzyme R44I, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0023
-
7,8-dihydrofolate mutant enzyme R44M, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0024
-
7,8-dihydrofolate mutant enzyme R44Q, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0025
-
7,8-dihydrofolate mutant enzyme R44K, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0025
-
7,8-dihydrofolate mutant enzyme R44N, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0025
-
7,8-dihydrofolate mutant enzyme R44T, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0027
-
7,8-dihydrofolate mutant enzyme R44F, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0029
-
7,8-dihydrofolate mutant enzyme R44P, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.003
-
7,8-dihydrofolate mutant enzyme R44D, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0031
-
7,8-dihydrofolate mutant enzyme R44S, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.0037
-
7,8-dihydrofolate mutant enzyme R44W, at 15°C, pH not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+ Escherichia coli
-
5,6,7,8-tetrahydrofolate + NADP+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+
-
Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.3 DHFR
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.3 0.3
-
7,8-dihydrofolate mutant enzyme R44P, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.69
-
7,8-dihydrofolate mutant enzyme R44D, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.89
-
7,8-dihydrofolate mutant enzyme R44E, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.89
-
7,8-dihydrofolate mutant enzyme R44Y, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 0.98
-
7,8-dihydrofolate mutant enzyme R44L, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1.15
-
7,8-dihydrofolate mutant enzyme R44I, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1.31
-
7,8-dihydrofolate mutant enzyme R44V, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1.39
-
7,8-dihydrofolate mutant enzyme R44F, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1.59
-
7,8-dihydrofolate mutant enzyme R44H, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1.78
-
7,8-dihydrofolate mutant enzyme R44G, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1.9
-
7,8-dihydrofolate mutant enzyme R44Q, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 2
-
7,8-dihydrofolate mutant enzyme R44T, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 2.41
-
7,8-dihydrofolate mutant enzyme R44W, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 2.43
-
7,8-dihydrofolate mutant enzyme R44C, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 3.05
-
7,8-dihydrofolate mutant enzyme R44A, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 3.3
-
7,8-dihydrofolate mutant enzyme R44N, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 3.8
-
7,8-dihydrofolate mutant enzyme R44M, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 5.4
-
7,8-dihydrofolate wild type enzyme, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 5.7
-
7,8-dihydrofolate mutant enzyme R44K, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 5.8
-
7,8-dihydrofolate mutant enzyme R44S, at 15°C, pH not specified in the publication Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADPH
-
Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.1.3 100
-
7,8-dihydrofolate mutant enzyme R44P, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 230
-
7,8-dihydrofolate mutant enzyme R44D, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 470
-
7,8-dihydrofolate mutant enzyme R44E, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 500
-
7,8-dihydrofolate mutant enzyme R44F, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 560
-
7,8-dihydrofolate mutant enzyme R44I, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 660
-
7,8-dihydrofolate mutant enzyme R44W, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 680
-
7,8-dihydrofolate mutant enzyme R44L, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 800
-
7,8-dihydrofolate mutant enzyme R44Q, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 800
-
7,8-dihydrofolate mutant enzyme R44T, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 900
-
7,8-dihydrofolate mutant enzyme R44Y, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1200
-
7,8-dihydrofolate mutant enzyme R44G, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1300
-
7,8-dihydrofolate mutant enzyme R44N, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1600
-
7,8-dihydrofolate mutant enzyme R44M, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1700
-
7,8-dihydrofolate mutant enzyme R44V, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1900
-
7,8-dihydrofolate mutant enzyme R44A, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 1900
-
7,8-dihydrofolate mutant enzyme R44S, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 2200
-
7,8-dihydrofolate mutant enzyme R44C, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 2300
-
7,8-dihydrofolate mutant enzyme R44K, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 2500
-
7,8-dihydrofolate mutant enzyme R44H, at 15°C, pH not specified in the publication Escherichia coli
1.5.1.3 3400
-
7,8-dihydrofolate wild type enzyme, at 15°C, pH not specified in the publication Escherichia coli