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Literature summary for 1.18.1.3 extracted from

  • Sielaff, B.; Andreesen, J.R.
    Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacterium sp. strain HE5 (2005), FEBS J., 272, 1148-1159.
    View publication on PubMed
Search for more literature for 1.18.1.3

Inhibitors

Inhibitors Comment Organism Structure
KCl sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above Mycobacterium sp.
NaCl sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above Mycobacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000037
-
 oxidized ferredoxin recombinant ferredoxin with C-terminal His-tag, pH 8.6 Mycobacterium sp.
0.0000053
-
 oxidized ferredoxin wild-type ferredoxin, pH 8.6 Mycobacterium sp.
0.0000105
-
 oxidized ferredoxin recombinant ferredoxin with N-terminal His-tag, pH 8.6 Mycobacterium sp.

Organism

Organism UniProt Comment Textmining
Mycobacterium sp.
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of P450-containing mono-oxygenase using purified homologous enzyme, ferrdoxin and P450 Mycobacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADH
-
 Mycobacterium sp. 2 ferrocytochrome c + NAD+ + H+
-
 ?
additional information no substrates of enzyme: morpholine, piperidine, pyrrolidine. Morpholine is a substrate of the P450mor system, consisting of enzyme, Fe3S4 ferredoxin and cytochrome P450 Mycobacterium sp. ?
-
 ?
NADH + nitroblue tetrazolium
-
 Mycobacterium sp. NAD+ + reduced nitroblue tetrazolium
-
 ?
oxidized ferredoxin + NADH + H+
-
 Mycobacterium sp. reduced ferredoxin + NAD+
-
 r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
-
 Mycobacterium sp.