Literature summary for 1.6.5.2 extracted from

Wolfova, J.; Brynda, J.; Mesters, J.R.; Carey, J.; Grandori, R.; Smatanova, I.K.
Crystallographic study of Escherichia coli flavoprotein WrbA, a new NAD(P)H-dependent quinone oxidoreductase (2008), Mater. Struct. Chem. Biol. Phys. Technol., 15, 55-57.

No PubMed abstract available

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Application

Application	Comment	Organism
biotechnology	the flavoprotein WrbA from Escherichia coli represents a new family of multimeric flavodoxin-like proteins implicated in cell protection against oxidative stress, WrbA has NAD(P)H: quinone reductase activity, forms multimers and binds FMN only weakly	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
with and without FMN using the sitting drop vapor-diffusion technique	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
21000	-	SDS-PAGE	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A8G6	-	-

Purification (Commentary)

Purification (Comment)	Organism
for crystallization	Escherichia coli

Synonyms

Synonyms	Comment	Organism
NADPH:quinone oxidoreductase	-	Escherichia coli
WrbA	has NAD(P)H:quinone reductase activity	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
FMN	-	Escherichia coli

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Release 2023.1 (January 2023)