2,5-dihydroxypyridine 5,6-dioxygenase

In enzymology, a 2,5-dihydroxypyridine 5,6-dioxygenase (EC 1.13.11.9) is an enzyme that catalyzes the chemical reaction

2,5-dihydroxypyridine + O₂ + H₂O maleamate + formate

The 3 substrates of this enzyme are 2,5-dihydroxypyridine, O₂, and H₂O, whereas its two products are maleamate and formate.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O₂ as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O₂. The systematic name of this enzyme class is 2,5-dihydroxypyridine:oxygen 5,6-oxidoreductase. Other names in common use include 2,5-dihydroxypyridine oxygenase, and pyridine-2,5-diol dioxygenase. This enzyme participates in nicotinate and nicotinamide metabolism. It employs one cofactor, iron.

References

IUBMB entry for 1.13.11.9
BRENDA references for 1.13.11.9 (Recommended.)
PubMed references for 1.13.11.9
PubMed Central references for 1.13.11.9
Google Scholar references for 1.13.11.9
BEHRMAN EJ, STANIER RY (1957). "The bacterial oxidation of nicotinic acid". J. Biol. Chem. 228: 923–45. PMID 13475371.
Gauthier JJ, Rittenberg SC (1971). "The metabolism of nicotinic acid. I. Purification and properties of 2,5-dihydroxypyridine oxygenase from Pseudomonas putida N-9". J. Biol. Chem. 246: 3737–42. PMID 5578917.
Gauthier JJ, Rittenberg SC (1971). "The metabolism of nicotinic acid. II. 2,5-dihydroxypyridine oxidation, product formation, and oxygen 18 incorporation". J. Biol. Chem. 246: 3743–8. PMID 5578918.