1.5.1.42: FMN reductase (NADH)
This is an abbreviated version!
For detailed information about FMN reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.42
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1.5.1.42
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luciferase
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monooxygenase
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desulfurization
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bioluminescent
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rhodococcus
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biodesulfurization
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erythropolis
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photobacterium
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dibenzothiophene
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fossil
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instantly
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p-hydroxyphenylacetate
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cost-competitive
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baumannii
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sigma54-dependent
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petroleum
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fmnh2-dependent
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phosphoreum
- 1.5.1.42
- luciferase
- monooxygenase
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desulfurization
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bioluminescent
- rhodococcus
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biodesulfurization
- erythropolis
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photobacterium
- dibenzothiophene
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fossil
-
instantly
- p-hydroxyphenylacetate
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cost-competitive
- baumannii
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sigma54-dependent
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petroleum
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fmnh2-dependent
- phosphoreum
Reaction
Synonyms
DszD, flavin reductase, Fred, HcbA3, hexachlorobenzene oxidative dehalogenase system reductase component, 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 (flavin reductase), NADH:FMN-oxidoreductase
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1.5.1.42 FMN reductase (NADH)Advanced search results
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General Information on EC 1.5.1.42 - FMN reductase (NADH)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
mutation of the critical residue Thr62, T62N and T62A, show a 5 and 7fold increase in catalytic rate, respectively
metabolism
physiological function
additional information
evolution
phylogenetic analysis demonstrats that Photobacterium leiognathi strain YL LuxG has a rather distant evolutionary relationship with Frase I of Aliivibrio fischeri and Frp of Vibrio harveyi, but a close evolutionary relationship with Fre from Escherichia coli, which are all enzymes related to oxidoreductases. Changes in the functionally conserved sites contribute to the functional divergence of LuxG and Fre. Bioinformatics analysis of LuxG sequences in bacteria, overview. Structure comparisons
evolution
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phylogenetic analysis demonstrats that Photobacterium leiognathi strain YL LuxG has a rather distant evolutionary relationship with Frase I of Aliivibrio fischeri and Frp of Vibrio harveyi, but a close evolutionary relationship with Fre from Escherichia coli, which are all enzymes related to oxidoreductases. Changes in the functionally conserved sites contribute to the functional divergence of LuxG and Fre. Bioinformatics analysis of LuxG sequences in bacteria, overview. Structure comparisons
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metabolism
the enzyme is involved in the degradation of (-)-camphor
metabolism
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the enzyme is involved in the degradation of (-)-camphor
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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
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NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence
physiological function
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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
DszD from Rhodococcus erythropolis is a NADH-FMN oxidoreductase responsible for supplying FMNH2 to DszA and DszC in the biodesulfurization process of crude oil, the 4S pathway. The rate-limiting step of the reduction of FMN to FMNH2 is a process catalysed by DszD and known to play an important role in the reaction energy profile
physiological function
LuxG supplies reduced flavin mononucleotide (FMN) for bacterial luminescence by catalyzing the oxidation of nicotinamide adenine dinucleotide hydrogen (NADH)
physiological function
Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). HcbA3 shows the highest affinity for FMN. HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653
physiological function
Rhodococcus erythropolis IGTS8 / ATCC 53968
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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
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physiological function
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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
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physiological function
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LuxG supplies reduced flavin mononucleotide (FMN) for bacterial luminescence by catalyzing the oxidation of nicotinamide adenine dinucleotide hydrogen (NADH)
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additional information
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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
critical role of the residue in position 62 (threonine) of the DszD sequence in the enzymatic activity. This residue is located near the N5 atom of the isoalloxazine ring of FMN. Structure modelling of wild-type and mutants using quantum mechanics/molecular mechanics (QM/MM) method, and active site as well as substrate binding structure analysis, overview
additional information
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critical role of the residue in position 62 (threonine) of the DszD sequence in the enzymatic activity. This residue is located near the N5 atom of the isoalloxazine ring of FMN. Structure modelling of wild-type and mutants using quantum mechanics/molecular mechanics (QM/MM) method, and active site as well as substrate binding structure analysis, overview
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
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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
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