Literature summary for 1.5.1.42 extracted from

Bezrukikh, A.; Esimbekova, E.; Nemtseva, E.; Kratasyuk, V.; Shimomura, O.
Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH FMN-oxidoreductase-luciferase (2014), Anal. Bioanal. Chem., 406, 5743-5747 .

Search for more literature for 1.5.1.42

Protein Variants

Protein Variants	Comment	Organism
additional information	design of a stable immobilizing reagent for bioluminescent analysis using luciferase, EC 1.14.14., from a recombinant Escherichia coli strain and NADH:FMN-oxidoreductase, EC 1.5.1.42. Natural polymers, gelatin and starch, are used to create a viscous, structured microenvironment for the NADH:FMN-oxidoreductase-luciferase system. Evaluation of the stability of the coupled enzyme system, overview. Both gelatin and starch have a stabilizing effect on the enzymes, the enzymes' activity is increased 2fold in the presence of 1% and 5% of gelatin at 20°C and 25°C, respectively. The acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol/l) is observed, thermal inactivation rate constants of the enzymes at 25-43°C are unchanged	Aliivibrio fischeri

General Stability

General Stability	Organism
immobilization in starch and gelatin gels increases the stability of of the enzme to the effects of external conditions	Aliivibrio fischeri

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Aliivibrio fischeri	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	lyophilized enzyme	Aliivibrio fischeri	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
NADH:FMN-oxidoreductase	-	Aliivibrio fischeri

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
20	-	enzyme immobilized in 1% of gelatin	Aliivibrio fischeri
25	-	enzyme immobilized in 5% of gelatin	Aliivibrio fischeri

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
10	43	effective rate constants of the first and second thermal inactivation stages of coupled enzymes NADH:FMN-oxidoreductase and luciferase in the presence of 1% gelatin, 5% gelatin, or buffer solution (control) at different temperatures, overview	Aliivibrio fischeri

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.8	-	free enzyme	Aliivibrio fischeri
7.2	-	gelatin-immobilized enzyme	Aliivibrio fischeri

pH Range

pH Minimum	pH Maximum	Comment	Organism
6.8	8.1	over 50% of maximal activity within this range	Aliivibrio fischeri

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Aliivibrio fischeri
NADH	-	Aliivibrio fischeri

General Information

General Information	Comment	Organism
physiological function	NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence	Aliivibrio fischeri

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Release 2023.1 (January 2023)