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Literature summary for 1.5.1.36 extracted from

  • Nijvipakul, S.; Ballou, D.P.; Chaiyen, P.
    Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity (2010), Biochemistry, 49, 9241-9248.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.36

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0027
-
 FMN at 4°C in 50 mM Tris-Cl buffer, pH 8.0 Photobacterium leiognathi
0.015
-
 NADH at 4°C in 50 mM Tris-Cl buffer, pH 8.0 Photobacterium leiognathi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FMN + NADH + H+ Photobacterium leiognathi
-
 FMNH2 + NAD+
-
 ?
riboflavin + NADH + H+ Photobacterium leiognathi
-
 reduced riboflavin + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Photobacterium leiognathi
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMN + NADH + H+
-
 Photobacterium leiognathi FMNH2 + NAD+
-
 ?
riboflavin + NADH + H+
-
 Photobacterium leiognathi reduced riboflavin + NAD+
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Photobacterium leiognathi

Synonyms

Synonyms Comment Organism
LuxG
-
 Photobacterium leiognathi
NADH:FMN oxidoreductase
-
 Photobacterium leiognathi

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7
-
 FMN at 4°C in 50 mM Tris-Cl buffer, pH 8.0 Photobacterium leiognathi

Cofactor

Cofactor Comment Organism Structure
NADH the enzyme prefers NADH as a substrate Photobacterium leiognathi