Tetrahydroxynaphthalene reductase

In enzymology, a tetrahydroxynaphthalene reductase (EC 1.1.1.252) is an enzyme that catalyzes the chemical reaction

scytalone + NADP⁺ 1,3,6,8-tetrahydroxynaphthalene + NADPH + H⁺

Thus, the two substrates of this enzyme are scytalone and NADP⁺, whereas its 3 products are 1,3,6,8-tetrahydroxynaphthalene, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is scytalone:NADP⁺ Delta5-oxidoreductase.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1DOH, 1G0N, and 1G0O.

References

• Wheeler MH; Greenblatt GA (1988). "The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease". Exp. Mycol. 12 (2): 151–160. doi:10.1016/0147-5975(88)90004-7. 
• Vidal-Cros A, Viviani F, Labesse G, Boccara M, Gaudry M (1994). "Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing". Eur. J. Biochem. 219 (3): 985–92. doi:10.1111/j.1432-1033.1994.tb18581.x. PMID 8112349. 
• Thompson JE, Basarab GS, Andersson A, Lindqvist Y, Jordan DB (1997). "Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism". Biochemistry. 36 (7): 1852–60. doi:10.1021/bi962355u. PMID 9048570.