Scytalone dehydratase

From Wikipedia, the free encyclopedia

In enzymology, a scytalone dehydratase (EC 4.2.1.94) is an enzyme that catalyzes the chemical reaction

scytalone $\rightleftharpoons$ 1,3,8-trihydroxynaphthalene + H₂O

Hence, this enzyme has one substrate, scytalone, and two products, 1,3,8-trihydroxynaphthalene and H₂O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is scytalone 7,8-hydro-lyase (1,3,8-trihydroxynaphthalene-forming). This enzyme is also called scytalone 7,8-hydro-lyase.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1IDP, 1STD, 2STD, 3STD, 4STD, 5STD, 6STD, and 7STD.

[edit] References

IUBMB entry for 4.2.1.94
BRENDA references for 4.2.1.94 (Recommended.)
PubMed references for 4.2.1.94
PubMed Central references for 4.2.1.94
Google Scholar references for 4.2.1.94
Butler MJ, Lazarovits G, Higgins VJ and Lachance M-A (1988). "Partial-purification and characterization of a dehydratase associated with the pentaketide melanogenesis pathway of Phaeococcomyces sp and other fungi". Exp. Mycol. 12: 367–376. doi:10.1016/0147-5975(88)90028-X.
Tajima S, Kubo Y, Furusawa I and Shishiyama J (1989). "Purification of a melanin biosynthetic enzyme converting scytalone to 1,3,8-trihydroxynaphthalene from Cochliobolus miyabeanus". Exp. Mycol. 13: 69. doi:10.1016/0147-5975(89)90009-1.
Wheeler MH and Greenblatt GA (1988). "The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease". Exp. Mycol. 12: 151–160. doi:10.1016/0147-5975(88)90004-7.