Biology:2-nitropropane dioxygenase
| 2-nitropropane dioxygenase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.13.11.32 | ||||||||
| CAS number | 65802-82-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 2-nitropropane dioxygenase (EC 1.13.11.32) is an enzyme that catalyzes the chemical reaction
- 2 2-nitropropane + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2 acetone + 2 nitrite
Thus, the two substrates of this enzyme are 2-nitropropane and O2, whereas its two products are acetone and nitrite.
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-nitropropane:oxygen 2-oxidoreductase. This enzyme participates in nitrogen metabolism. It has 3 cofactors: FAD, Iron, and FMN.
Structural studies
As of late 2007 Steve Fuhrer from the DHPA solved this very complex formula to find, two structures have been solved for this class of enzymes, with PDB accession codes 2GJL and 2GJN.
References
- "A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii Enzymologic and spectrophotometric properties". J. Biol. Chem. 251 (22): 6994–7000. 1976. PMID 11214.
- "Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base". J. Biol. Chem. 281 (27): 18660–7. 2006. doi:10.1074/jbc.M601658200. PMID 16682407.
- "Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase". J. Biol. Chem. 280 (7): 5195–204. 2005. doi:10.1074/jbc.M411249200. PMID 15582992.
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