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Information on EC 1.5.1.42 - FMN reductase (NADH)
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1.5.1.42 FMN reductase (NADH)IUBMB Comments
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].
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Word Map
- 1.5.1.42
- luciferase
- monooxygenase
-
bioluminescent
-
desulfurization
- rhodococcus
-
biodesulfurization
-
photobacterium
- erythropolis
- dibenzothiophene
-
fossil
-
cost-competitive
-
fmnh2-dependent
- p-hydroxyphenylacetate
-
instantly
- baumannii
-
sigma54-dependent
-
petroleum
- phosphoreum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
DszD, flavin reductase, Fred, LuxG, LuxG oxidoreductase, NADH specific FMN reductase, NADH-dependent FMN reductase, NADH-FMN oxidoreductase, NADH-FMN reductase, NADH:flavin oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DszD
flavin reductase
Fred
LuxG
LuxG oxidoreductase
NADH specific FMN reductase
NADH-dependent FMN reductase
-
-
-
-
NADH-FMN oxidoreductase
NADH-FMN reductase
-
-
-
-
NADH:flavin oxidoreductase
-
-
-
-
NADH:FMN oxidoreductase
NADH:FMN oxidoreductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NAD+ = FMN + NADH + H+
-
-
-
-
FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
-
FMNH2 + NAD+ = FMN + NADH + H+
catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview
-
FMNH2 + NAD+ = FMN + NADH + H+
catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
-
FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
-
-
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PATHWAY SOURCE
PATHWAYS
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FAD + NADH + H+
FADH2 + NAD+
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
-
-
?
FAD + NADH + H+
FADH2 + NAD+
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
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
activity with FADH2 and NAD+ is 5% of the activity with FMNH2 and NAD+
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
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 + NADH + H+
FMNH2 + NAD+
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 + NADH + H+
FMNH2 + NAD+
-
activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
-
-
?
additional information
?
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
activity with FAD and NADPH is 0.5% of the activity with FMNH2 and NAD+
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADH
-
the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
NADPH
-
activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADPH
-
the NADH specific FMN reductase does does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by: 0.000325 M dicoumarol, 10 mM KCN, 1% Triton X-100
-
additional information
-
no inhibition by 0.01 mM 2,4-dinitrophenol, 0.2 mM dicoumarol, 0.1 mM rotenone
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Riboflavin Deficiency
Effect of riboflavin deficiency on activity of NADH-FMN oxidoreductase (ferriductase) and iron content of rat liver.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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
-
additional information
additional information
-
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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
-
additional information
additional information
-
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
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
purity was too low to permit estimation of specific activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
bimodal, pH 5: 90% of maximal activity, pH 6.5: about 50% of maximal activity, pH 10: about 70% of maximal activity
5 - 8.6
-
the pH curve is bimodal, with maximal activity exhibited at pH 8.6, a minimum at pH 6.0. and a second maximum at pH 5.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
additional information
additional information
stopped-flow kinetic experiments are performed at 4°C
additional information
-
stopped-flow kinetic experiments are performed at 4°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
the enzyme is involved in the degradation of (-)-camphor
metabolism
-
the enzyme is involved in the degradation of (-)-camphor
-
physiological function
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
physiological function
-
NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence
physiological function
-
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
physiological function
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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
-
physiological function
-
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
-
additional information
-
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
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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
-
Show AA Sequence and Transmembrane Helices (1817 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T62A
-
the mutant shows 7fold increase in activity compared to the wild type enzyme
T62N
-
the mutant shows 5fold increase in activity compared to the wild type enzyme
T62A
-
the mutant shows 7fold increase in activity compared to the wild type enzyme
-
T62N
-
the mutant shows 5fold increase in activity compared to the wild type enzyme
-
additional information
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
additional information
-
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
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
25
the enzyme irreversibly unfolds with a half-life of about 80 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization in starch and gelatin gels increases the stability of of the enzme to the effects of external conditions
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, in presence of 2 mM dithiothreitol, stable over several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene luxG encoding LuxG, the flavin reductase, is encoded in the same operon as its counterpart LuxAB
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gerlo, E.; Charlier, J.
Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi
Eur. J. Biochem.
57
461-467
1975
Vibrio harveyi
brenda
Jablonski, E.; DeLuca, M.
Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi
Biochemistry
16
2932-2936
1977
Vibrio harveyi, Vibrio harveyi No. 392
brenda
Izumoto, Y.; Mori, T.; Yamamoto, K.
Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase from Vibrio harveyi
Biochim. Biophys. Acta
1185
243-246
1994
Vibrio harveyi (P43127)
brenda
Uetz, T.; Schneider, R.; Snozzi, M.; Egli, T.
Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600
J. Bacteriol.
174
1179-1188
1992
Aminobacter aminovorans
brenda
Duane, W.; Hastings, J.W.
Flavin mononucleotide reductase of luminous bacteria
Mol. Cell. Biochem.
6
53-64
1975
Vibrio harveyi
brenda
Kamali, N.; Tavallaie, M.; Bambai, B.; Karkhane, A.A.; Miri, M.
Site-directed mutagenesis enhances the activity of NADH-FMN oxidoreductase (DszD) activity of Rhodococcus erythropolis
Biotechnol. Lett.
32
921-927
2010
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 (ATCC 53968)
brenda
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
Anal. Bioanal. Chem.
406
5743-5747
2014
Aliivibrio fischeri
brenda
Tinikul, R.; Pitsawong, W.; Sucharitakul, J.; Nijvipakul, S.; Ballou, D.P.; Chaiyen, P.
The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion
Biochemistry
52
6834-6843
2013
Photobacterium leiognathi (P29237), Photobacterium leiognathi, Photobacterium leiognathi TH1 (P29237), Photobacterium leiognathi TH1
brenda
Sousa, S.F.; Sousa, J.F.; Barbosa, A.C.; Ferreira, C.E.; Neves, R.P.; Ribeiro, A.J.; Fernandes, P.A.; Ramos, M.J.
Improving the biodesulfurization of crude oil and derivatives a QM/MM investigation of the catalytic mechanism of NADH-FMN oxidoreductase (DszD)
J. Phys. Chem. A
120
5300-5306
2016
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
brenda
Iwaki, H.; Grosse, S.; Bergeron, H.; Leisch, H.; Morley, K.; Hasegawa, Y.; Lau, P.C.
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
Appl. Environ. Microbiol.
79
3282-3293
2013
Pseudomonas putida (M4YFG7), Pseudomonas putida ATCC 17453 (M4YFG7)
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