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.

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 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.1 With NAD⁺ or NADP⁺ as acceptor

                1.5.1.36 flavin reductase (NADH)

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Results	in table
8	Activating Compound
1935	AA Sequence
6	Application
19	Cloned(Commentary)
34	Cofactor
3	Crystallization (Commentary)
5	Expression
19	General Information
35	Inhibitors
7	kcat/KM [mM/s]
4	Ki Value [mM]
28	KM Value [mM]
2	Localization
6	Metals/Ions
12	Molecular Weight [Da]
30	Natural Substrates/ Products (Substrates)
66	Organism
2	Pathway
4	PDB ID
11	pH Optimum
3	pH Range
2	pI Value
16	Protein Variants
16	Purification (Commentary)
4	Reaction
40	Reference
2	Renatured (Commentary)
3	Source Tissue
10	Specific Activity [micromol/min/mg]
2	Storage Stability
75	Substrates and Products (Substrate)
33	Subunits
84	Synonyms
1	Systematic Name
11	Temperature Optimum [°C]
1	Temperature Stability [°C]
11	Turnover Number [1/s]

Application

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Application on EC 1.5.1.36 - flavin reductase (NADH)

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

Acinetobacter baumannii

Q6Q271

amperometric NADH biosensor system that employs the allosterically modulated reductase component of the 4-hydroxyphenylacetate hydroxylase in an adapted osmium(III)-complex-modified redox polymer film for analyte quantification. The activity of the reductase is enhanced upon binding of effector 4-hydroxy-phenylacetic acid, allowing the acceleration of the substrate conversion rate on the sensor surface by in situ addition or preincubation with 4-hydroxy-phenylacetic acid. Acceleration of NADH oxidation amplifies the response of the biosensor, with a 1.5fold increase in the sensitivity of analyte detection

763881

synthesis

5 entries

synthesis

Acinetobacter baumannii

Q6Q271

generation of FMNH2 by enzyme encapsulated in poly(lactide-co-glycolide) nanoparticles. Enzymatic activity, stability, and reusability of the nanoparticles prepared using three different methods [(o/w), water in oil in water (w/o/w), and solid in oil in water (s/o/w)] are compared. The solid in oil in water method provides the optimal conditions for encapsulation of the reudctase, giving the highest enzyme activity, stability, and reusability. The solid in oil in water method improves enzyme activity about 11-and 9fold compared to water in oil in water and oil in water methods. Solid in oil in water nanoparticles can be reused 14 times with nearly 50% activity remaining

764823

synthesis

Escherichia coli

A0A140NG67

in vivo production of ortho-hydroxylated flavonoids by recombinant Escherichia coli. When HpaC is linked with an S-Tag on the C terminus, the enzyme activity is significantly affected. The optimal culture conditions are a substrate concentration of 80 mg/l, an induction temperature of 28°C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. The efficiency of eriodictyol conversion from recombinant strains fed naringin is up to 57.67. Highest conversion efficiencies for production of catechin and caffeate are 35.2 % and 32.93%, respectively

765429

synthesis

Escherichia coli

A0A140NG67

overexpression of the HpaB and HpaC genes in Saccharomyces cerevisiae achieves hydroxytyrosol titers of 1.15 mg/l and 4.6 mg/l in a minimal medium in which either 1 mM tyrosine or 1 mM tyrosol are respectively added

764691

synthesis

Escherichia coli BL21-DE3

-

overexpression of the HpaB and HpaC genes in Saccharomyces cerevisiae achieves hydroxytyrosol titers of 1.15 mg/l and 4.6 mg/l in a minimal medium in which either 1 mM tyrosine or 1 mM tyrosol are respectively added

-

synthesis

Escherichia coli BL21-DE3

-

in vivo production of ortho-hydroxylated flavonoids by recombinant Escherichia coli. When HpaC is linked with an S-Tag on the C terminus, the enzyme activity is significantly affected. The optimal culture conditions are a substrate concentration of 80 mg/l, an induction temperature of 28°C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. The efficiency of eriodictyol conversion from recombinant strains fed naringin is up to 57.67. Highest conversion efficiencies for production of catechin and caffeate are 35.2 % and 32.93%, respectively

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