Paromamine 6'-oxidase
| Paromamine 6'-oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.3.43 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| 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] It catalyses the following chemical reaction
paromamine
O2
H2O2
6'-oxoparomamine
The enzyme characterised from Streptomyces fradiae uses molecular oxygen to convert the primary alcohol of the glucosamine sugar unit into its aldehyde, giving hydrogen peroxide as a byproduct.[2] This is a step in the biosynthesis of several aminoglycoside antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.[3][4]
References
- ↑ Enzyme 1.1.3.43 at KEGG Pathway Database.
- ↑ Huang F, Spiteller D, Koorbanally NA, Li Y, Llewellyn NM, Spencer JB (February 2007). "Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin". ChemBioChem. 8 (3): 283–8. doi:10.1002/cbic.200600371. PMID 17206729.
- ↑ Yu Y, Hou X, Ni X, Xia H (February 2008). "Biosynthesis of 3'-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption". The Journal of Antibiotics. 61 (2): 63–9. doi:10.1038/ja.2008.111. PMID 18408324.
- ↑ Clausnitzer D, Piepersberg W, Wehmeier UF (September 2011). "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. doi:10.1111/j.1365-2672.2011.05082.x. PMID 21689223.
External links
- Paromamine+6'-oxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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