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NAD(P)H-dependent oxidoreductase
This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species [1]. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy [1]. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP [2]. This family is related to Pfam:PF03358 and Pfam:PF00258. [1]. 7568029. The three-dimensional structure of NAD(P)H:quinone reductase, a. flavoprotein involved in cancer chemoprotection and. chemotherapy: mechanism of the two-electron reduction. Li R, Bianchet MA, Talalay P, Amzel LM;. Proc Natl Acad Sci U S A 1995;92:8846-8850.. [2]. 2168383. Isolation and properties of acyl carrier protein. phosphodiesterase of Escherichia coli.. Fischl AS, Kennedy EP;. J Bacteriol 1990;172:5445-5449. (from Pfam)
NADPH-dependent FMN reductase
Members of this protein family use NAD(P)H to reduce FMN and regenerate FMNH2. Members include the homodimeric, NAD(P)H-dependent enzyme SsuE from Escherichia coli, which serves as a partner to an FMNH2-dependent alkanesulfonate monooxygenase. It is induced by sulfate starvation. The NADH-dependent enzyme MsuE from Pseudomonas aeruginosa is outside the scope of this model (see model TIGR03566).
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