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Literature summary 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 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.42 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

EC Number General Stability Organism
1.5.1.42 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.42 Aliivibrio fischeri
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.5.1.42 NADH:FMN-oxidoreductase
-
Aliivibrio fischeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.42 20
-
enzyme immobilized in 1% of gelatin Aliivibrio fischeri
1.5.1.42 25
-
enzyme immobilized in 5% of gelatin Aliivibrio fischeri

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.42 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.42 6.8
-
free enzyme Aliivibrio fischeri
1.5.1.42 7.2
-
gelatin-immobilized enzyme Aliivibrio fischeri

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.5.1.42 6.8 8.1 over 50% of maximal activity within this range Aliivibrio fischeri

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.42 NAD+
-
Aliivibrio fischeri
1.5.1.42 NADH
-
Aliivibrio fischeri

General Information

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