In enzymology, juglone 3-monooxygenase (EC 1.14.99.27) is an enzyme that catalyzes the chemical reaction
juglone 3-monooxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.99.27 | ||||||||
CAS no. | 98865-54-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- 5-hydroxy-1,4-naphthoquinone + AH2 + O2 3,5-dihydroxy-1,4-naphthoquinone + A + H2O
The 3 substrates of this enzyme are 5-hydroxy-1,4-naphthoquinone, AH2, and O2, whereas its 3 products are 3,5-dihydroxy-1,4-naphthoquinone, A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is 5-hydroxy-1,4-naphthoquinone,hydrogen-donor:oxygen oxidoreductase (3-hydroxylating). Other names in common use include juglone hydroxylase, naphthoquinone hydroxylase, and naphthoquinone-hydroxylase.
References
edit- Rettenmaier H, Lingens F (1985). "Purification and some properties of two isofunctional juglone hydroxylases from Pseudomonas putida J1". Biol. Chem. Hoppe-Seyler. 366 (7): 637–46. doi:10.1515/bchm3.1985.366.2.637. PMID 4041238.