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l136 |
Description |
UDP-4-dehydro-6-deoxy-D-glucose aminotransferase (2.6.1.-) |
Alternative names |
UDP-4-keto-6-deoxy-D-glucose-oxoglutarate aminotransferase;
UDP-viosamine--glutamate aminotransferase;
L136
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Catalyzed reaction |
UDP-4-dehydro-6-deoxy-D-glucose + L-glutamate = UDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate. |
Cofactor |
Pyridoxal phosphate. |
Comments |
The only functionally validated enzyme enzyme is from the giant Mimivirus, which infects several Acanthamoeba species. Apparently viosamine, the final product of the pathway involving L136, is used by this virus to form glycosylated fibers - resembling polysaccharides from bacterial cell walls - that cover the virion and promote phagocytosis by the host cells.
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Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) l136
BRENDA (activities) l136
KEGG (pathways) l136
PLPMDB (PLP mutants) l136
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References |
Piacente F, De Castro C, Jeudy S, Gaglianone M, Laugieri ME, Notaro A, Salis A, Damonte G, Abergel C, Tonetti MG (2017) The rare sugar N-acetylated viosamine is a major component of Mimivirus fibers J. Biol.Chem. 292 7385-7394. Piacente F, Marin M, Molinaro A, De Castro C, Seltzer V, Salis A, Damonte G, Bernardi C, Claverie JM, Abergel C, Tonetti M. (2012) Giant DNA virus mimivirus encodes pathway for biosynthesis of unusual sugar 4-amino-4,6-dideoxy-D-glucose (Viosamine) J. Biol.Chem. 287 73009-18. Articles on l136 |
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last changed |
2017/08/07 13:05 |
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