“Tetrahydroxynaphthalene reductase”的意思、由来-开放百科全书

词条

Tetrahydroxynaphthalene reductase

释义

Structural studies
References

{{enzyme
| Name = tetrahydroxynaphthalene reductase
| EC_number = 1.1.1.252
| CAS_number = 153702-05-7
| IUBMB_EC_number = 1/1/1/252
| GO_code = 0047039
| image =
| width =
| caption =
}}

In enzymology, a tetrahydroxynaphthalene reductase ({{EC number|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 {{PDB link|1DOH}}, {{PDB link|1G0N}}, and {{PDB link|1G0O}}.

References

{{cite journal |author1 = Wheeler MH |author2 =Greenblatt GA | date = 1988 | title = The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease | journal = Exp. Mycol. | volume = 12 | pages = 151–160 | doi = 10.1016/0147-5975(88)90004-7 | issue = 2 }}
{{cite journal | vauthors = Vidal-Cros A, Viviani F, Labesse G, Boccara M, Gaudry M | date = 1994 | title = Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing | journal = Eur. J. Biochem. | volume = 219 | pages = 985–92 | pmid = 8112349 | doi = 10.1111/j.1432-1033.1994.tb18581.x | issue = 3 }}
{{cite journal | vauthors = Thompson JE, Basarab GS, Andersson A, Lindqvist Y, Jordan DB | date = 1997 | title = Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism | journal = Biochemistry | volume = 36 | pages = 1852–60 | pmid = 9048570 | doi = 10.1021/bi962355u | issue = 7 }}

3 : EC 1.1.1|NADPH-dependent enzymes|Enzymes of known structure

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