UDP-4-amino-4-deoxy-L-arabinose aminotransferase
| UDP-4-amino-4-deoxy-L-arabinose aminotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.87 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-4-amino-4-deoxy-L-arabinose aminotransferase (EC 2.6.1.87, UDP-(beta-L-threo-pentapyranosyl-4-ulose diphosphate) aminotransferase, UDP-4-amino-4-deoxy-L-arabinose---oxoglutarate aminotransferase, UDP-Ara4O aminotransferase, UDP-L-Ara4N transaminase) is an enzyme with systematic name UDP-4-amino-4-deoxy-beta-L-arabinose:2-oxoglutarate aminotransferase.[1][2] This enzyme catalyses the following chemical reaction
- UDP-4-amino-4-deoxy-beta-L-arabinopyranose + 2-oxoglutarate UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
This protein is a pyridoxal 5'-phosphate enzyme.
References
[edit]- ^ Breazeale SD, Ribeiro AA, Raetz CR (July 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-deoxyl-L-arabinose". The Journal of Biological Chemistry. 278 (27): 24731–9. doi:10.1074/jbc.m304043200. PMID 12704196.
- ^ Noland BW, Newman JM, Hendle J, Badger J, Christopher JA, Tresser J, Buchanan MD, Wright TA, Rutter ME, Sanderson WE, Müller-Dieckmann HJ, Gajiwala KS, Buchanan SG (November 2002). "Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme". Structure. 10 (11): 1569–80. doi:10.1016/s0969-2126(02)00879-1. PMID 12429098.
External links
[edit]- UDP-4-amino-4-deoxy-L-arabinose+aminotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
