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B6db activities: 2.6.1.87

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.
Catalyzed reaction UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate <=> UDP-beta-L-threo-pentapyranos-4-ulose + glutamate
Cofactor Pyridoxal phosphate.
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
 

Family 

2.6.1.87 (9)
 
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
 
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
 
last changed 2014/02/18 18:16

B6db activities