The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD+ oxidoreductase
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s
LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s
bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview
Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC
Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC
bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview
the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A
the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A
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
the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate
the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate
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
to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, recombinant plasmids expressing Fred (FMN reductase (NADH)) in tandem with the respective 2,5-diketocamphane- and 3,6-diketocamphane 1,2-monooxygenase-encoding genes in Escherichia coli are constructed
Camphor pathway redux functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions