The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.6.1.93     
Accepted name: neamine transaminase
Reaction: neamine + 2-oxoglutarate = 6′-dehydroparomamine + L-glutamate
For diagram of neamine and ribostamycin biosynthesis, click here
Other name(s): glutamate—6′-dehydroparomamine aminotransferase; btrB (gene name); neoN (gene name); kacL (gene name)
Systematic name: neamine:2-oxoglutarate aminotransferase
Comments: The reaction occurs in vivo in the opposite direction. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin B, butirosin, neomycin and ribostamycin. Works in combination with EC 1.1.3.43, paromamine 6-oxidase, to replace the 6′-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces kanamyceticus can also catalyse EC 2.6.1.94, 2′-deamino-2′-hydroxyneamine transaminase, which leads to production of kanamycin A [3]. The enzyme from the bacterium Streptomyces fradiae can also catalyse EC 2.6.1.95, leading to production of neomycin C [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
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. [PMID: 17206729]
2.  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. [PMID: 21689223]
3.  Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [PMID: 21983602]
[EC 2.6.1.93 created 2012]
 
 


Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald