1.5.1.36: flavin reductase (NADH)
This is an abbreviated version!
For detailed information about flavin reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.36
-
1.5.1.36
-
nadph:flavin
-
fmnh2
-
alkanesulfonate
-
oxygen-insensitive
-
beneckea
-
desulfonation
-
nitroreductases
-
fmnh2-dependent
- 1.5.1.36
-
nadph:flavin
- fmnh2
-
alkanesulfonate
-
oxygen-insensitive
-
beneckea
-
desulfonation
- nitroreductases
-
fmnh2-dependent
Reaction
Synonyms
AbeF, BaiH, BorF, C1-HpaH, DszD, FAD reductase, FerA, flavin mononucleotide reductase, flavin reductase, flavin:NADH oxidoreductase, FMN reductase, Frd188, frd2, fre, HpaC, LJ0548, LJ0549, LJ_0548, LJ_0549, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H-flavin oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H:flavin-oxidoreductase, NADH-dependent flavin reductase, NADH-flavin oxidoreductase, NADH: flavin oxidoreductase, NADH: flavinoxidore ductase/NADH oxidase, NADH:flavin oxidoreductase, NADH:FMN oxidoreductase, nfr1, nfr2, NOX, Pden2689, SMOB-ADP1
ECTree
1.5.1.36 flavin reductase (NADH)Advanced search results
results (
results (Engineering
Engineering on EC 1.5.1.36 - flavin reductase (NADH)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E248A
residue of the of the recognition helix of the MarR domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type, high constitutive NADH oxidation activity without auto-inhibition
E251A
residue of the of the recognition helix of the MarR domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type, high constitutive NADH oxidation activity without auto-inhibition
F216A
high constitutive NADH oxidation activity without auto-inhibition
H170A
putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type
N174A
putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type
R20A
residue of flavin reductase domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type
S172A
putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type
Y207A
putative residue of the 4-hydroxyphenylacetic acid binding site, no activation by 4-hydroxyphenylacetic acid along with low NADH oxidation rate
synthesis
additional information
synthesis
construction of biosynthetic pathways for the production of tyrosol acetate and hydroxytyrosol acetate in Escherichia coli. Escherichia coli YeaE is the best aldehyde reductase for tyrosol accumulation. Tyrosol acetate production is achieved by overexpression of alcohol acetyltransferase ATF1 from Saccharomyces cerevisiae, and hydroxytyrosol acetate production by overexpression of 4-hydroxyphenylacetate 3-hydroxylase genes HpaBC
synthesis
-
construction of biosynthetic pathways for the production of tyrosol acetate and hydroxytyrosol acetate in Escherichia coli. Escherichia coli YeaE is the best aldehyde reductase for tyrosol accumulation. Tyrosol acetate production is achieved by overexpression of alcohol acetyltransferase ATF1 from Saccharomyces cerevisiae, and hydroxytyrosol acetate production by overexpression of 4-hydroxyphenylacetate 3-hydroxylase genes HpaBC
-
additional information
-
improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
additional information
-
improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
-
additional information
-
construction of an HpaC inactivation mutant strain W-KO
additional information
-
site-directed mutagenesis of BorF implicates His160 and Arg38 as contributing to the catalytic activity and the pH dependence
additional information
site-directed mutagenesis of BorF implicates His160 and Arg38 as contributing to the catalytic activity and the pH dependence
