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2.6.1.87 |
Description |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase |
Alternative names |
UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase;
UDP-4-amino-4-deoxy-L-arabinose aminomutase;
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase;
UDP-Ara4O aminotransferase;
UDP-L-Ara4N transaminase;
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
aminotransferase;
ArnB;
PmrH.
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Catalyzed reaction |
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate <=> UDP-beta-L-threo-pentapyranos-4-ulose + glutamate |
Cofactor |
Pyridoxal phosphate. |
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ArnB catalyzes the transfer of the amino group from glutamic acid to the 4"-position of a UDP-linked ketopyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose. In turn, 4-amino-4-deoxy-L-arabinose is used by pathogenic bacteria such as Salmonella to modify Lipid A, conferring resistance to cationic antimicrobial peptides, including those derived from the innate immune system. |
PDB |
1MDX; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.6.1.87
BRENDA (activities) 2.6.1.87
KEGG (pathways) 2.6.1.87
PLPMDB (PLP mutants) 2.6.1.87
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References |
Breazeale, S.D.; Ribeiro, A.A.; Raetz, C.R. (2003) Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli. An aminotransferase (ArnB) that generates UDP-4-amino-4-deoxyl-L-arabinose
J Biol Chem 278 24731-9. Noland, B.W., Newman, J.M.; Hendle, J.; Badger J.; Christopher, J.A.; Tresser, J.; Buchanan, M.D.; Wright, T.A.; Rutter, M.E.; Sanderson, W.E.; Muller-Dieckmann, H.J.; Gajiwala, K.S.; Buchanan, S.G. (2002) Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme
Structure (Camb) 10 1569-80. Articles on 2.6.1.87 |
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last changed |
2019/12/11 17:14 |
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