The Enzyme Database

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Accepted name: paromamine 6′-oxidase
Reaction: paromamine + O2 = 6′-dehydroparomamine + H2O2
Other name(s): btrQ (gene name); neoG (gene name); kanI (gene name); tacB (gene name); neoQ (obsolete gene name)
Systematic name: paromamine:oxygen 6′-oxidoreductase
Comments: Contains FAD. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Works in combination with EC, neamine transaminase, to replace the 6′-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces fradiae also catalyses EC, 6′′′-hydroxyneomycin C oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem 8 (2007) 283–288. [DOI] [PMID: 17206729]
2.  Yu, Y., Hou, X., Ni, X. and Xia, H. Biosynthesis of 3′-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption. J. Antibiot. (Tokyo) 61 (2008) 63–69. [DOI] [PMID: 18408324]
3.  Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6′-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642–651. [DOI] [PMID: 21689223]
[EC created 2012]

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