| http://purl.uniprot.org/citations/8366124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8366124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/8366124 | http://www.w3.org/2000/01/rdf-schema#comment | "UDP-N-acetylglucosamine acyltransferase of Escherichia coli catalyzes the reaction, UDP-GlcNAc + R-3-hydroxymyristoyl-ACP--> UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc + ACP. Using Matrex Gel Green A and heparin-agarose, we have purified the enzyme to near homogeneity from a strain that overproduces it 474-fold. The subunit molecular mass determined by SDS-gel electrophoresis is approximately 30 kDa, consistent with results of previous radiolabeling experiments in mini-cells. The amino-terminal sequence (Met-Ile-Asp-Lys-Ser-Ala-Phe-Val-His-Pro) and the amino acid composition of the purified protein are consistent with DNA sequencing (Coleman, J., and Raetz, C. R. H. (1988) J. Bacteriol. 170, 1268-1274). At saturating concentrations of the second substrate, the apparent Km values for UDP-GlcNAc and R-3-hydroxymyristoyl-ACP are 99 and 1.6 microM, respectively. There is an absolute requirement for the R-3-hydroxy moiety of the fatty acyl-ACP substrate; myristoyl-ACP binds effectively (IC50 = 2 microM) but is inactive (< 0.01%) as an alternate substrate. The most remarkable feature of the reaction is its unfavorable equilibrium constant, Keq approximately equal to 0.01, which is not predicted by model S-->O acyl transfer reactions. Thus, although UDP-GlcNAc acyltransferase catalyzes the first unique step of lipid A biosynthesis, it is the second enzyme (the deacetylase) that commits the substrates to this pathway. The specific activity of the deacetylase is elevated approximately 5-fold when lipid A synthesis is inhibited."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)36592-5"xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)36592-5"xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Raetz C.R."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Mohan S."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Anderson M.S."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Bull H.G."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Galloway S.M."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Kelly T.M."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/author | "Radika K."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/pages | "19858-19865"xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/title | "UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable."xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://purl.uniprot.org/core/volume | "268"xsd:string |
| http://purl.uniprot.org/citations/8366124 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8366124 |
| http://purl.uniprot.org/citations/8366124 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8366124 |
| http://purl.uniprot.org/citations/8366124 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8366124 |
| http://purl.uniprot.org/citations/8366124 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8366124 |
| http://purl.uniprot.org/enzyme/2.3.1.129 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8366124 |
| http://purl.uniprot.org/uniprot/P0A722#attribution-ECA7F053AA40955B067F4CA6AB9FE673 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8366124 |