L-ornithine N5 monooxygenase

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L-ornithine N5 monooxygenase
4nzh2.jpg
Ornithine monooxygenase tetramer, Aspergillus fumigatus
Identifiers
EC number1.14.13.196
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

In enzymology, an ornithine monooxygenase (EC 1.14.13.196) is an enzyme that catalyzes the chemical reaction

L-ornithine + NAD(P)H + O2 N(5)-hydroxy-L-ornithine + NAD(P)+ + H2O

Thus, the three substrates of this enzyme are L-ornithine, NAD(P)H and O2, whereas its three products are N(5)-hydroxy-L-ornithine, NAD(P)+ and H2O. The coenzyme is FAD.

This enzyme belongs to the family of oxidoreductases, specifically the monooxygenases. The systematic name of this enzyme class is L-ornithine N5 monooxygenase (flavin-dependent). The enzyme from the pathogenic fungus Aspergillus fumigatus catalyzes a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics.

Structural studies[edit]

As of late 2013, 8 structures have been solved for this class of enzymes, with PDB accession codes 4NZH, 4B63, 4B64, 4B65, 4B66, 4B67, 4B68 and 4B69.

References[edit]

  • Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A (2012). "Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases". Biochemistry. 51: 7043–5. PMID 22928747.
  • http://www.jbc.org/content/early/2013/09/26/jbc.M113.487181.full.pdf