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Literature summary for 1.18.1.3 extracted from

  • Broadus, R.M.; Haddock, J.D.
    Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400 (1998), Arch. Microbiol., 170, 106-112.
    View publication on PubMed
Search for more literature for 1.18.1.3

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.058
-
 NADH reaction with 2,6-dichlorophenolindophenol Pseudomonas sp.
0.156
-
 NADPH reaction with 2,6-dichlorophenolindophenol Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41500
-
 NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, gel filtration Pseudomonas sp.
43600
-
 1 * 43600, NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, SDS-PAGE Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp.
-
 NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase
-
Pseudomonas sp. LB400
-
-
-

Purification (Commentary)

Purification (Comment) Organism
NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Pseudomonas sp. 2 ferrocyanide + NAD+ + H+
-
 ?
2 ferricyanide + NADH
-
 Pseudomonas sp. LB400 2 ferrocyanide + NAD+ + H+
-
 ?
2 ferricytochrome c + NADH
-
 Pseudomonas sp. 2 ferrocytochrome c + NAD+ + H+
-
 ?
2 ferricytochrome c + NADH
-
 Pseudomonas sp. LB400 2 ferrocytochrome c + NAD+ + H+
-
 ?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
 Pseudomonas sp. NAD+ + reduced 2,6-dichlorophenolindophenol
-
 ?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
-
 Pseudomonas sp. LB400 NAD+ + reduced 2,6-dichlorophenolindophenol
-
 ?
NADH + oxidized nitro blue tetrazolium + H+
-
 Pseudomonas sp. NAD+ + reduced nitro blue tetrazolium
-
 ?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
-
 Pseudomonas sp. NADP+ + reduced 2,6-dichlorophenolindophenol
-
 ?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
-
 Pseudomonas sp. LB400 NADP+ + reduced 2,6-dichlorophenolindophenol
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 43600, NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, SDS-PAGE Pseudomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
32
-
 reduction of 2,6-dichlorophenolindophenol Pseudomonas sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
 no activity detected at 5°C or at 55°C. Activity at 50°C is 15.2% of maximal activity Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 reduction of 2,6-dichlorophenolindophenol Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD contains 0.89 mol of FAD per mol of enzyme Pseudomonas sp.
NADH
-
 Pseudomonas sp.
NADPH
-
 Pseudomonas sp.