Biology:UDP-4-amino-4-deoxy-L-arabinose aminotransferase
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UDP-4-amino-4-deoxy-L-arabinose aminotransferase | |||||||||
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Identifiers | |||||||||
EC number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
This protein is a pyridoxal 5'-phosphate enzyme.
References
- ↑ "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. July 2003. doi:10.1074/jbc.m304043200. PMID 12704196.
- ↑ "Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme". Structure 10 (11): 1569–80. November 2002. doi:10.1016/s0969-2126(02)00879-1. PMID 12429098.
External links
- UDP-4-amino-4-deoxy-L-arabinose+aminotransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/UDP-4-amino-4-deoxy-L-arabinose aminotransferase.
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