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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/8555230 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8555230 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8555230 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/8555230 | http://www.w3.org/2000/01/rdf-schema#comment | "The GlmU protein is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities which catalyzes the transformation of glucosamine-1-P, UTP, and acetyl-CoA to UDP-N-acetylglucosamine [Mengin-Lecreulx, D., & van Heijenoort, J. (1994) J. Bacteriol. 176, 5788-5795], a fundamental precursor in bacterial peptidoglycan biosynthesis and the source of activated N-acetylglucosamine in lipopolysaccharide biosynthesis in Gram-negative bacteria. In the work described here, the GlmU protein and truncation variants of GlmU (N- and C-terminal) were purified and kinetically characterized for substrate specificity and reaction order. It was determined that the GlmU protein first catalyzed acetyltransfer followed by uridylyltransfer. The N-terminal portion of the enzyme was capable of only uridylyltransfer, and the C-terminus catalyzed only acetyltransfer. GlmU demonstrated a 12-fold kinetic preference (kcat/Km, 3.1 x 10(5) versus 2.5 x 10(4) L.mol-1.s-1) for acetyltransfer from acetyl-CoA to glucosamine-1-P as compared to UDP-glucosamine. No detectable uridylyltransfer from UTP to glucosamine-1-P was observed in the presence of GlmU; however, the enzyme was competent in catalyzing the formation of UDP-N-acetylglucosamine from UTP and N-acetylglucosamine-1-P (kcat/Km 1.2 x 10(6) L.mol-1.s-1). A two active site model for the GlmU protein was indicated both by domain dissection experiments and by assay of the bifunctional reaction. Kinetic studies demonstrated that a pre-steady-state lag in the production of UDP-N-acetylglucosamine from acetyl-CoA, UTP, and glucosamine-1-P was due to the release and accumulation of steady-state levels of the intermediate N-acetylglucosamine-1-P."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi952275a"xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi952275a"xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Gehring A.M."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Gehring A.M."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Walsh C.T."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Walsh C.T."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Brown E.D."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Brown E.D."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Lees W.J."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Lees W.J."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Mindiola D.J."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/author | "Mindiola D.J."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/pages | "579-585"xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/pages | "579-585"xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/title | "Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/title | "Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/8555230 | http://purl.uniprot.org/core/volume | "35"xsd:string |