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Literature summary for 1.19.1.1 extracted from

  • Leadbeater, C.; McIver, L.; Campopiano, D.; Webster, S.; Baxter, R.; Kelly, S.; Price, N.; Lysek, D.; Noble, M.; Chapman, S.; Munro, A.
    Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase (2000), Biochem. J., 352, 257-266.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.19.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modelling indicates that movement of the C-terminal tryptophan (W248) is necessary to permit close approach of the nicotinamide ring of NADPH to the flavin. Residues R174 and R184 are located close to the adenosine ribose 2'-phosphate group, and R144 is likely to interact with the nicotinamide ribose 5'-phosphate group Escherichia coli

Protein Variants

Protein Variants Comment Organism
R144A mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH Escherichia coli
R174A mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH Escherichia coli
R184A mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0017
-
 NADH mutant R184A, pH 7.5, 30°C Escherichia coli
0.002
-
 NADH wild-type, pH 7.5, 30°C Escherichia coli
0.0039
-
 NADPH wild-type, pH 7.5, 30°C Escherichia coli
0.0051
-
 NADH mutant R144A, pH 7.5, 30°C Escherichia coli
0.0053
-
 NADPH mutant R144A, pH 7.5, 30°C Escherichia coli
0.0099
-
 NADH mutant R174A, pH 7.5, 30°C Escherichia coli
0.0202
-
 NADPH mutant R174A, pH 7.5, 30°C Escherichia coli
0.0544
-
 NADPH mutant R184A, pH 7.5, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli HMS174
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxidized cytochrome c + NADH + H+
-
 Escherichia coli reduced cytochrome c + NAD+
-
 r
oxidized cytochrome c + NADH + H+
-
 Escherichia coli HMS174 reduced cytochrome c + NAD+
-
 r
oxidized cytochrome c + NADPH + H+
-
 Escherichia coli reduced cytochrome c + NADP+
-
 r
oxidized cytochrome c + NADPH + H+
-
 Escherichia coli HMS174 reduced cytochrome c + NADP+
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.23
-
 NADH mutant R144A, pH 7.5, 30°C Escherichia coli
0.55
-
 NADH wild-type, pH 7.5, 30°C Escherichia coli
0.71
-
 NADH mutant R174A, pH 7.5, 30°C Escherichia coli
0.84
-
 NADH mutant R184A, pH 7.5, 30°C Escherichia coli
2.2
-
 NADPH mutant R174A, pH 7.5, 30°C Escherichia coli
4.03
-
 NADPH mutant R144A, pH 7.5, 30°C Escherichia coli
5.1
-
 NADPH mutant R184A, pH 7.5, 30°C Escherichia coli
5.65
-
 NADPH wild-type, pH 7.5, 30°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
93
-
 NADPH mutant R184A, pH 7.5, 30°C Escherichia coli
108
-
 NADPH mutant R174A, pH 7.5, 30°C Escherichia coli
270
-
 NADH wild-type, pH 7.5, 30°C Escherichia coli
445
-
 NADH mutant R144A, pH 7.5, 30°C Escherichia coli
506
-
 NADH mutant R184A, pH 7.5, 30°C Escherichia coli
715
-
 NADH mutant R174A, pH 7.5, 30°C Escherichia coli
762
-
 NADPH mutant R144A, pH 7.5, 30°C Escherichia coli
1448
-
 NADPH wild-type, pH 7.5, 30°C Escherichia coli