Biology:Paromamine 6'-oxidase
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Short description: Class of enzymes
| Paromamine 6'-oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.3.43 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Paromamine 6'-oxidase (EC 1.1.3.43, btrQ (gene), neoG (gene), kanI (gene), tacB (gene)) is an enzyme with systematic name paromamine:oxygen 6'-oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- paromamine + O2 6'-dehydroparomamine + H2O2
This enzymes participates in biosynthesis of several aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
References
- ↑ "Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin". ChemBioChem 8 (3): 283–8. February 2007. doi:10.1002/cbic.200600371. PMID 17206729.
- ↑ "Biosynthesis of 3'-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption". The Journal of Antibiotics 61 (2): 63–9. February 2008. doi:10.1038/ja.2008.111. PMID 18408324.
- ↑ "The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin". Journal of Applied Microbiology 111 (3): 642–51. September 2011. doi:10.1111/j.1365-2672.2011.05082.x. PMID 21689223.
External links
- Paromamine+6'-oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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