EC 1.1.3.43 - Paromamine 6'-oxidase

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IntEnz Enzyme Nomenclature
EC 1.1.3.43

Names

Accepted name:
paromamine 6'-oxidase
Other names:
btrQ (gene name)
neoG (gene name)
kanI (gene name)
tacB (gene name)
neoQ (obsolete gene name)
Systematic name:
paromamine:oxygen 6'-oxidoreductase

Reaction

Cofactor

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 2.6.1.93, neamine transaminase, to replace the 6-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 1.1.3.44, 6'''-hydroxyneomycin C oxidase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Huang, F., Spiteller, D., Koorbanally, N. A., Li, Y., Llewellyn, N. M., Spencer, J. B.
    Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin.
    Chembiochem 8: 283-288 (2007). [PMID: 17206729]
  2. Yu, Y., Hou, X., Ni, X., Xia, H.
    Biosynthesis of 3'-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption.
    J. Antibiot. 61: 63-69 (2008). [PMID: 18408324]
  3. Clausnitzer, D., Piepersberg, W., 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: 642-651 (2011). [PMID: 21689223]

[EC 1.1.3.43 created 2012]