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 | Organism |
---|---|
immobilization in starch and gelatin gels increases the stability of of the enzme to the effects of external conditions | Aliivibrio fischeri |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMNH2 + NAD+ | Aliivibrio fischeri | - |
FMN + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aliivibrio fischeri | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | lyophilized enzyme | Aliivibrio fischeri | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMNH2 + NAD+ | - |
Aliivibrio fischeri | FMN + NADH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
NADH:FMN-oxidoreductase | - |
Aliivibrio fischeri |
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 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
free enzyme | Aliivibrio fischeri |
7.2 | - |
gelatin-immobilized enzyme | Aliivibrio fischeri |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.8 | 8.1 | over 50% of maximal activity within this range | Aliivibrio fischeri |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Aliivibrio fischeri | |
NADH | - |
Aliivibrio fischeri |
General Information | Comment | Organism |
---|---|---|
physiological function | NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence | Aliivibrio fischeri |