1.5.1.38: FMN reductase (NADPH)

This is an abbreviated version!
For detailed information about FMN reductase (NADPH), go to the full flat file.

Reaction

Synonyms

(NADPH)-dependent flavin mononucleotide reductase, (NADPH)-dependent FMN reductase, BC_1619, EC 1.5.1.29, EC 1.6.8.1, flavin reductase P, FMN reductase, FRP, More, NAD(P)H:FMN reductase, NADPH specific FMN reductase, NADPH-flavin oxidoreductase, NADPH-FMN oxidoreductase, NADPH:FMN oxidoreductase, NADPH:FMN reductase, SsuE, ssueE, ycbP, ydgI

ECTree

1 Oxidoreductases

1.5 Acting on the CH-NH group of donors

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.1.38 FMN reductase (NADPH)

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Results	in table
4073	AA Sequence
7	Cloned(Commentary)
16	Cofactor
3	Crystallization (Commentary)
11	General Information
9	Inhibitors
13	kcat/KM [mM/s]
28	KM Value [mM]
18	Molecular Weight [Da]
12	Natural Substrates/ Products (Substrates)
17	Organism
4	Pathway
31	PDB ID
8	pH Optimum
1	pH Range
10	Protein Variants
10	Purification (Commentary)
6	Reaction
17	Reference
1	Renatured (Commentary)
3	Specific Activity [micromol/min/mg]
2	Storage Stability
36	Substrates and Products (Substrate)
12	Subunits
42	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
1	Temperature Stability [°C]
8	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.5.1.38 - FMN reductase (NADPH)

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purified recombinant enzyme in apoform, or complexed with FMN or FMNH2, hanging drop vapour diffusion method, mixing 0.004 ml of 10 mg/ml of protein in 10 mM HEPES, pH 7.0, with 0.002 ml of reservoir solution containing 7.5% w/v PEG 3350 and 0.1 M sodium citrate, at room temperature, for complexed protein, the crystals are soaked in an AML containing 1 mM FMN solution, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution

Escherichia coli

P80644

741896

vapor-diffusion technique yields single crystals that grow as hexagonal rods and diffract to 2.9 A resolution using synchrotron X-ray radiation. The protein crystallizes in the primitive hexagonal space group P622. Substitution of two leucine residues (Leu114 and Leu165) to methionine is performed to obtain selenomethionine-containing SsuE for MAD phasing. The selenomethionine derivative of SsuE has been expressed and purified and crystals of the protein have been obtained with and without bound FMN

Escherichia coli

713622

the 1.8 A crystal structure of flavin reductase P from Vibrio harVeyi is solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A(2) of surface area buried in the dimer interface. Each subunit comprises two domains

Vibrio harveyi

Q56691

392299