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Literature summary for 1.18.1.6 extracted from

  • McLean, K.J.; Scrutton, N.S.; Munro, A.W.
    Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA (2003), Biochem. J., 372, 317-327.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene fprA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme contains a second, kinetically distinct and inhibitory pyridine nucleotide-binding site Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information transient and steady-state kinetics of diaphorase and flavin reductase activities, determination of reduction potential Mycobacterium tuberculosis
0.0041
-
NADPH diaphorase activity with ferricyanide, pH 7.2, 30°C Mycobacterium tuberculosis
0.051
-
NADH diaphorase activity with ferricyanide, pH 7.2, 30°C Mycobacterium tuberculosis
0.16
-
ferricyanide pH 7.2, 30°C Mycobacterium tuberculosis
2.5
-
oxidized 2,6-dichloroindophenol pH 7.2, 30°C Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49357
-
x * 49357, recombinant enzyme, mass spectrometry Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced ferredoxin + NAD(P)+ Mycobacterium tuberculosis
-
oxidized ferredoxin + NAD(P)H
-
r

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIQ3 gene fprA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli to homogeneity Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADPH diaphorase activity Mycobacterium tuberculosis 2 ferrocyanide + NADP+ + H+
-
?
ferricyanide + NADH
-
Mycobacterium tuberculosis ferrocyanide + NAD+ + H+
-
r
additional information the enzyme contains a second, kinetically distinct and inhibitory pyridine nucleotide-binding site Mycobacterium tuberculosis ?
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol diaphorase activity Mycobacterium tuberculosis NADP+ + reduced 2,6-dichlorophenolindophenol
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH
-
Mycobacterium tuberculosis reduced 2,6-dichlorophenolindophenol + NADP+ + H+
-
r
reduced ferredoxin + NAD(P)+
-
Mycobacterium tuberculosis oxidized ferredoxin + NAD(P)H
-
r

Subunits

Subunits Comment Organism
? x * 49357, recombinant enzyme, mass spectrometry Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ferredoxin reductase
-
Mycobacterium tuberculosis
FprA
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.011
-
oxidized 2,6-dichlorophenolindophenol pH 7.2, 30°C Mycobacterium tuberculosis
25.6
-
NADH flavin reduction, pH 7.2, 30°C Mycobacterium tuberculosis
33.7
-
ferricyanide pH 7.2, 30°C Mycobacterium tuberculosis
50.6
-
NADPH flavin reduction, pH 7.2, 30°C Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
FAD flavoenzyme, determination of reduction potential Mycobacterium tuberculosis
additional information the enzyme contains a second, kinetically distinct and inhibitory pyridine nucleotide-binding site Mycobacterium tuberculosis
NAD(P)+ preference for NADP+ Mycobacterium tuberculosis