1.5.1.39: FMN reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about FMN reductase [NAD(P)H], go to the full flat file.
Reaction
Synonyms
ChuY, EC 1.5.1.29, EC 1.6.8.1, flavin mononucleotide reductase, FMN reductase, fre, FRG, H2O-forming FOR, LrFOR, NAD(P)H-flavin reductase, NAD(P)H:FMN-oxidoreductase, NADH: FMN oxidoreductase, NADPH-dependent FMN reductase, NfoR, non-specific NAD(P)H-FMN reductase, pden_5119, Red, SsuE, two-component FMN-dependent monooxygenase, water forming NADH: FMN oxidoreductase
ECTree
1.5.1.39 FMN reductase [NAD(P)H]Advanced search results
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results (Engineering
Engineering on EC 1.5.1.39 - FMN reductase [NAD(P)H]
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Y118A
site-directed mutagenesis, the structure of the Y118A SsuE Pi-helix is converted to an alpha-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the Pi-helix is altered, the FMN binding region remains unchanged. The mutant forms dimers in contrast to the wild-type
N173A
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site-directed mutagenesis, the mutant shows 66% reduced activity compared to wild-type enzyme
T29A
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site-directed mutagenesis, the mutant shows 2.91fold increased activity compared to the wild-type enzyme
T29D
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site-directed mutagenesis, the mutant shows 3.9fold increased activity compared to the wild-type enzyme
T29G
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site-directed mutagenesis, the mutant shows 3.7fold increased activity compared to the wild-type enzyme
T29N
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site-directed mutagenesis, the mutant shows 2.2fold increased activity compared to the wild-type enzyme
T29R
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site-directed mutagenesis, the mutant shows 90% reduced activity compared to wild-type enzyme
T29Y
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site-directed mutagenesis, the mutant shows 40% reduced activity compared to wild-type enzyme
N173A
Lacticaseibacillus rhamnosus ATCC 53103
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site-directed mutagenesis, the mutant shows 66% reduced activity compared to wild-type enzyme
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additional information
additional information
construction of a DELTA118 SsuE enzyme mutant, which forms dimers in contrast to the wild-type. The Pi-helices do not contribute to the dimeric assembly, and the variants show no difference at the dimeric interface compared to wild-type. Deletion of Tyr118 (DELTAY118 SsuE) also eliminates reductase activity, but this variant is tetrameric in solution. Comparison of wild-type and Y118A variants of SsuE with related wild-type and mutant H126Y MsuE from Pseudomonas fluorescens (EC 1.5.1.42), overview
additional information
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a small size or electronegative of residue in position 29 shortens the distance of NADH and FMN, promoting the electrons transfer and resulting in the increased activity
additional information
Lacticaseibacillus rhamnosus ATCC 53103
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a small size or electronegative of residue in position 29 shortens the distance of NADH and FMN, promoting the electrons transfer and resulting in the increased activity
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additional information
inactivation of the pden_5119 gene by insertion of a kanamycin resistance marker. Based on the IC50 values, the wild-type strain is 17.6, 4.1, and 9.5fold less sensitive to methyl viologen, diamide, and t-butyl hydroperoxide, respectively, compared to the mutant strain, demonstrating a stress protective capacity of the Pden_5119 protein. The Pden_5119 mutant displays decreased growth rate and increased growth yield. Changes in growth on alkanesulfonates and sulfate occurring as a result of mutation
additional information
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inactivation of the pden_5119 gene by insertion of a kanamycin resistance marker. Based on the IC50 values, the wild-type strain is 17.6, 4.1, and 9.5fold less sensitive to methyl viologen, diamide, and t-butyl hydroperoxide, respectively, compared to the mutant strain, demonstrating a stress protective capacity of the Pden_5119 protein. The Pden_5119 mutant displays decreased growth rate and increased growth yield. Changes in growth on alkanesulfonates and sulfate occurring as a result of mutation
additional information
-
inactivation of the pden_5119 gene by insertion of a kanamycin resistance marker. Based on the IC50 values, the wild-type strain is 17.6, 4.1, and 9.5fold less sensitive to methyl viologen, diamide, and t-butyl hydroperoxide, respectively, compared to the mutant strain, demonstrating a stress protective capacity of the Pden_5119 protein. The Pden_5119 mutant displays decreased growth rate and increased growth yield. Changes in growth on alkanesulfonates and sulfate occurring as a result of mutation
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