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

Contents

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.

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<span class="mw-page-title-main">2,6-Dihydroxypyridine</span> Chemical compound

2,6-Dihydroxypyridine is an alkaloid with the molecular formula C5H3N(OH)2. It is a colorless solid. 2,6-Dihyroxypyridine is an intermediate in the degradation of nicotine.

Alpha-ketoglutarate-dependent hydroxylases are a major class of non-heme iron proteins that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations. Functionally, the αKG-dependent hydroxylases are comparable to cytochrome P450 enzymes. Both use O2 and reducing equivalents as cosubstrates and both generate water.

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 (inactive 2024-09-12). ISSN   0892-6638 . Retrieved 13 February 2017.{{cite journal}}: CS1 maint: DOI inactive as of September 2024 (link)

Further reading