Salicylate 1-monooxygenase

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In enzymology, a salicylate 1-monooxygenase (EC 1.14.13.1) is an enzyme that catalyzes the chemical reaction

salicylate + NADH + 2 H⁺ + O₂ $\rightleftharpoons$ catechol + NAD⁺ + H₂O + CO₂

The 4 substrates of this enzyme are salicylate, NADH, H⁺, and O₂, whereas its 4 products are catechol, NAD⁺, H₂O, and CO₂.

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 O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating). Other names in common use include salicylate hydroxylase, salicylate 1-hydroxylase, salicylate monooxygenase, and salicylate hydroxylase (decarboxylating). This enzyme participates in 3 metabolic pathways: 1- and 2-methylnaphthalene degradation, naphthalene and anthracene degradation, and fluorene degradation. It employs one cofactor, FAD.

[edit] References

IUBMB entry for 1.14.13.1
BRENDA references for 1.14.13.1 (Recommended.)
PubMed references for 1.14.13.1
PubMed Central references for 1.14.13.1
Google Scholar references for 1.14.13.1
Suzuki K, Takemori S and Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. IV. Fluorimetric analysis of the complex formation". Biochim. Biophys. Acta 191: 77–85.
Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex". Biochim. Biophys. Acta. 191: 58–68. PMID 4898626.
Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M (1969). "Mechanism of the salicylate hydroxylase reaction. 3 Characterization and reactivity of chemically or photochemically reduced enzyme-flavin". Biochim. Biophys. Acta. 191: 69–76. PMID 4309912.
Yamamoto S, Katagiri M, Maeno H and Hayaishi O (1965). "Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide". J. Biol. Chem. 240: 3408–3413.