B6db activities : 2_6_1

	Activities \| Families \| Sequences \| Fold types \| References \| Help


	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 (0)

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	2019/12/11 17:14

Family