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Literature summary extracted from

  • Sielaff, B.; Andreesen, J.R.
    Analysis of the nearly identical morpholine monooxygenase-encoding mor genes from different Mycobacterium strains and characterization of the specific NADH: ferredoxin oxidoreductase of this cytochrome P450 system (2005), Microbiology, 151, 2593-2603.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.3 42396
-
1 * 42396, calculated, 1 * 50000, SDS-PAGE Mycobacterium sp.
1.18.1.3 50000
-
gel filtration Mycobacterium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.3 Mycobacterium sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.3 2 ferricyanide + NADH
-
Mycobacterium sp. 2 ferrocyanide + NAD+ + H+
-
?
1.18.1.3 2 ferricytochrome c + NADH
-
Mycobacterium sp. 2 ferrocytochrome c + NAD+ + H+
-
?
1.18.1.3 ferricytochrome c + NADH
-
Mycobacterium sp. ferrocytochrome c + NAD+ + H+
-
r

Subunits

EC Number Subunits Comment Organism
1.18.1.3 monomer 1 * 42396, calculated, 1 * 50000, SDS-PAGE Mycobacterium sp.
1.18.1.3 More enzyme interacts functionally with its redox partner, the Fe3S4 protein ferredoxin, and with the Fe2S2 protein adrenodoxin. Ferredoxin requires its specific NADH:ferredoxin reductase from the P450 system for efficient catalytic function Mycobacterium sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.3 4.5
-
ferricytochrome c pH 8.5, 30°C Mycobacterium sp.
1.18.1.3 60.2
-
ferricyanide pH 8.5, 30°C Mycobacterium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.3 FAD spectral maxima at 273, 378 and 452 nm, 0.75 mol of FAD per mol of protein Mycobacterium sp.