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2,5-dihydroxypyridine 5,6-dioxygenase

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2,5-dihydroxypyridine 5,6-dioxygenase
Identifiers
EC no.1.13.11.9
CAS no.9029-57-6
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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 N-formylmaleamic acid

The 2 substrates of this enzyme are 2,5-dihydroxypyridine and O2, whereas its product is N-formylmaleamic acid.[1]

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. It employs one cofactor, iron.

This enzyme participates in nicotinate and nicotinamide metabolism.[2]

Nomenclature

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.

References

  1. ^ Q88FY1
  2. ^ Henke, Matthew T.; Snider, Mark J. (1 April 2011). "Mechanistic studies of 2,5-dihydroxypyridine 5,6-dioxygenase (NicX) from Bordetella bronchiseptica". The FASEB Journal. 25 (1 Supplement): 714.2. doi:10.1096/fasebj.25.1_supplement.714.2. ISSN 0892-6638. Retrieved 13 February 2017.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Further reading

  • Behrman EJ, Stanier RY (1957). "The bacterial oxidation of nicotinic acid". J. Biol. Chem. 228 (2): 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 (11): 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 (11): 3743–8. PMID 5578918.
  • Behrman EJ (November 2008). "N-Formylmaleamic acid: an intermediate in nicotinic acid metabolism". Proc. Natl. Acad. Sci. U.S.A. 105 (47): E88, author reply E89. doi:10.1073/pnas.0808695105. PMC 2587544. PMID 19020104.