|
type |
Journal Article |
authors |
Huang F, Spiteller D, Koorbanally NA, Li Y, Llewellyn NM, Spencer JB.
|
title |
Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. |
journal |
Chembiochem |
Activity |
2.6.1.93 |
Family |
2.6.1.93 |
sel |
selected |
ui |
17206729 |
year |
(2007) |
volume |
8 |
number |
3 |
pages |
283-8 |
| |
abstract |
The proteins Neo-11 and Neo-18 encoded in the neomycin gene cluster (neo) of Streptomyces fradiae NCIMB 8233 have been characterized as glucosaminyl-6'-oxidase and 6'-oxoglucosaminyl:L-glutamate aminotransferase, respectively. The joint activity of Neo-11 and Neo-18 is responsible for the conversion of paromamine to neamine in the biosynthetic pathway of neomycin through a mechanism of FAD-dependent dehydrogenation followed by a pyridoxal-5'-phosphate-mediated transamination. Neo-18 is also shown to catalyze deamination at C-6''' of neomycin, thus suggesting bifunctional roles of the two enzymes in the formation of both neosamine rings of neomycin. The product of the btrB gene, a homologue of neo-18 in the butirosin biosynthetic gene cluster (btr) in Bacillus circulans, exhibits the same activity as Neo-18; this indicates that there is a similar reaction sequence in both butirosin and neomycin biosynthesis.
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last changed |
2016/10/03 12:18 |
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