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Literature summary for 1.5.1.3 extracted from

  • Horiuchi, Y.; Ohmae, E.; Tate, S.; Gekko, K.
    Coupling effects of distal loops on structural stability and enzymatic activity of Escherichia coli dihydrofolate reductase revealed by deletion mutants (2010), Biochim. Biophys. Acta, 1804, 846-855.
    View publication on PubMed
Search for more literature for 1.5.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli HB101 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
DELTAAla145 the mutant shows increased catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAArg52 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAArg52/DELTAAla145 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAArg52/DELTAGly121 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAArg52/DELTAGly67 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAGly121 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAGly121/DELTAAla145 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAGly67 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAGly67/DELTAAla145 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
DELTAGly67/DELTAGly121 the mutant shows reduced catalytic efficiency compared to the wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0008
-
 7,8-dihydrofolate deletion mutant DELTAAla145, at pH 7.0 and 25°C Escherichia coli
0.0013
-
 7,8-dihydrofolate wild type enzyme, at pH 7.0 and 25°C Escherichia coli
0.0048
-
 7,8-dihydrofolate deletion mutant DELTAGly67/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
0.0051
-
 7,8-dihydrofolate deletion mutant DELTAGly67, at pH 7.0 and 25°C Escherichia coli
0.0056
-
 7,8-dihydrofolate deletion mutant DELTAGly67/DELTAGly121, at pH 7.0 and 25°C Escherichia coli
0.0073
-
 7,8-dihydrofolate deletion mutant DELTAGly121/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
0.0108
-
 7,8-dihydrofolate deletion mutant DELTAGly121, at pH 7.0 and 25°C Escherichia coli
0.0502
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAGly67, at pH 7.0 and 25°C Escherichia coli
0.0512
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAGly121, at pH 7.0 and 25°C Escherichia coli
0.0777
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
0.1161
-
 7,8-dihydrofolate deletion mutant DELTAArg52, at pH 7.0 and 25°C 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 P0ABQ4
-
-

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
0.22
-
 7,8-dihydrofolate deletion mutant DELTAGly121/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
0.37
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAGly121, at pH 7.0 and 25°C Escherichia coli
0.38
-
 7,8-dihydrofolate deletion mutant DELTAGly67/DELTAGly121, at pH 7.0 and 25°C Escherichia coli
1.7
-
 7,8-dihydrofolate deletion mutant DELTAGly121, at pH 7.0 and 25°C Escherichia coli
16.5
-
 7,8-dihydrofolate deletion mutant DELTAGly67, at pH 7.0 and 25°C Escherichia coli
23.1
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAGly67, at pH 7.0 and 25°C Escherichia coli
24
-
 7,8-dihydrofolate deletion mutant DELTAAla145, at pH 7.0 and 25°C Escherichia coli
24.8
-
 7,8-dihydrofolate wild type enzyme, at pH 7.0 and 25°C Escherichia coli
31.9
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
41.1
-
 7,8-dihydrofolate deletion mutant DELTAGly67/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
96.3
-
 7,8-dihydrofolate deletion mutant DELTAArg52, at pH 7.0 and 25°C 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
10
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAGly121, at pH 7.0 and 25°C Escherichia coli
30
-
 7,8-dihydrofolate deletion mutant DELTAGly121/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
70
-
 7,8-dihydrofolate deletion mutant DELTAGly67/DELTAGly121, at pH 7.0 and 25°C Escherichia coli
160
-
 7,8-dihydrofolate deletion mutant DELTAGly121, at pH 7.0 and 25°C Escherichia coli
410
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
460
-
 7,8-dihydrofolate deletion mutant DELTAArg52/DELTAGly67, at pH 7.0 and 25°C Escherichia coli
830
-
 7,8-dihydrofolate deletion mutant DELTAArg52, at pH 7.0 and 25°C Escherichia coli
3300
-
 7,8-dihydrofolate deletion mutant DELTAGly67, at pH 7.0 and 25°C Escherichia coli
8600
-
 7,8-dihydrofolate deletion mutant DELTAGly67/DELTAAla145, at pH 7.0 and 25°C Escherichia coli
19200
-
 7,8-dihydrofolate wild type enzyme, at pH 7.0 and 25°C Escherichia coli
29400
-
 7,8-dihydrofolate deletion mutant DELTAAla145, at pH 7.0 and 25°C Escherichia coli