6-hydroxynicotinate dehydrogenase
| 6-hydroxynicotinate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.17.3.3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
6-hydroxynicotinate dehydrogenase (EC 1.17.3.3) is an enzyme that catalyzes the chemical reaction
6-hydroxyniacin
O2 + H2O
H2O2
2,6-dihydroxynicotinic acid
The three substrates of this enzyme are 6-hydroxyniacin, water, and oxygen. Its products are 2,6-dihydroxynicotinic acid and hydrogen peroxide.[1]
The enzyme isolated from Bacillus niacini is an oxidoreductase that contains an iron–sulfur cluster and uses flavin adenine dinucleotide and molybdenum.[2] The systematic name of this enzyme class is 6-hydroxynicotinate:O2 oxidoreductase. Other names in common use include 6-hydroxynicotinic acid hydroxylase, 6-hydroxynicotinic acid dehydrogenase, and 6-hydroxynicotinate hydroxylase.[3]
References
- ↑ Nagel M, Andreesen JR (1989). "Molybdenum-dependent degradation of nicotinic acid by Bacillus sp. DSM 2923". FEMS Microbiol. Lett. 59 (1–2): 147–152. doi:10.1111/j.1574-6968.1989.tb03099.x.
- ↑ Nagel M, Andreesen JR (1990). "Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini". Arch. Microbiol. 154 (6): 605–613. Bibcode:1990ArMic.154..605N. doi:10.1007/BF00248844.
- ↑ Enzyme 1.17.3.3 at KEGG Pathway Database.
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