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Literature summary for 1.5.1.39 extracted from

  • Govorun, A.; Esimbekova, E.; Kratasyuk, V.
    NAD(P)H FMN-oxidoreductase functioning under macromolecular crowding inxa0vitro modeling (2019), Dokl. Biochem. Biophys., 486, 213-215 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FMN + NADH + H+ Aliivibrio fischeri
-
FMNH2 + NAD+
-
r
FMN + NADPH + H+ Aliivibrio fischeri
-
FMNH2 + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Aliivibrio fischeri P43126
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMN + NADH + H+
-
Aliivibrio fischeri FMNH2 + NAD+
-
r
FMN + NADPH + H+
-
Aliivibrio fischeri FMNH2 + NADP+
-
r

Synonyms

Synonyms Comment Organism
fre
-
Aliivibrio fischeri
NAD(P)H-flavin reductase UniProt Aliivibrio fischeri
NAD(P)H:FMN-oxidoreductase
-
Aliivibrio fischeri
Red
-
Aliivibrio fischeri

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 40
-
Aliivibrio fischeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Aliivibrio fischeri

Cofactor

Cofactor Comment Organism Structure
NADH
-
Aliivibrio fischeri
NADPH
-
Aliivibrio fischeri

General Information

General Information Comment Organism
additional information the functioning of NAD(P)H:FMN-oxidoreductase (Red) from Vibrio fischeri is not affected under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin). The functioning of Red both under conditions of MMC and in diluted solutions is the same Aliivibrio fischeri