Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
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Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.Lipopolysaccharide endotoxinsA web server for predicting inhibitors against bacterial target GlmU proteinAcyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferaseCrystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+Structural basis of Synercid (quinupristin-dalfopristin) resistance in Gram-positive bacterial pathogensOpen and closed structures of the UDP-glucose pyrophosphorylase from Leishmania majorCrystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanismStructure of theE. colibifunctional GlmU acetyltransferase active site with substrates and productsStructural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferaseCharacterization of substrate binding and catalysis in the potential antibacterial targetN-acetylglucosamine-1-phosphate uridyltransferase (GlmU)Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding siteStructure and function of GlmU fromMycobacterium tuberculosisStructure ofN-acetylglucosamine-1-phosphate uridyltransferase (GlmU) fromMycobacterium tuberculosisin a cubic space groupCrystal Structure and Acyl Chain Selectivity of Escherichia coli LpxD, the N -Acyltransferase of Lipid A BiosynthesisCatalytic Mechanism of Perosamine N -Acetyltransferase Revealed by High-Resolution X-ray Crystallographic Studies and Kinetic AnalysesActivity and Crystal Structure of Arabidopsis thaliana UDP- N -Acetylglucosamine AcyltransferaseAn aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding modeExpression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferaseEvidence that WbpD is an N-acetyltransferase belonging to the hexapeptide acyltransferase superfamily and an important protein for O-antigen biosynthesis in Pseudomonas aeruginosa PAO1Kinetic and physical characterization of the inducible UDP-N-acetylglucosamine pyrophosphorylase from Giardia intestinalis.High-throughput screening identifies novel inhibitors of the acetyltransferase activity of Escherichia coli GlmU.Crystal structure of potato tuber ADP-glucose pyrophosphorylase.Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7.Osmotically induced synthesis of the dipeptide N-acetylglutaminylglutamine amide is mediated by a new pathway conserved among bacteria.Enzymatic route to preparative-scale synthesis of UDP-GlcNAc/GalNAc, their analogues and GDP-fucoseBiosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose in Aneurinibacillus thermoaerophilus L420-91T.Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction.The bacterial cell wall as a source of antibacterial targets.Biosynthetic enzymes of unusual microbial sugars.Three monophyletic superfamilies account for the majority of the known glycosyltransferases.Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host.Thermodynamics of binding of divalent magnesium and manganese to uridine phosphates: implications for diabetes-related hypomagnesaemia and carbohydrate biocatalysisStructure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide.ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis.Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA)Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU).Preliminary crystallographic analysis of ADP-glucose pyrophosphorylase from Agrobacterium tumefaciens.Enzymatic synthesis and properties of uridine-5'-O-(2-thiodiphospho)-N-acetylglucosamine.Substrate-bound crystal structures reveal features unique to Mycobacterium tuberculosis N-acetyl-glucosamine 1-phosphate uridyltransferase and a catalytic mechanism for acetyl transfer.
P2860
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P2860
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structure of the Escherichia c ...... acetyltransferase active sites
@ast
Structure of the Escherichia c ...... acetyltransferase active sites
@en
Structure of the Escherichia c ...... acetyltransferase active sites
@nl
type
label
Structure of the Escherichia c ...... acetyltransferase active sites
@ast
Structure of the Escherichia c ...... acetyltransferase active sites
@en
Structure of the Escherichia c ...... acetyltransferase active sites
@nl
prefLabel
Structure of the Escherichia c ...... acetyltransferase active sites
@ast
Structure of the Escherichia c ...... acetyltransferase active sites
@en
Structure of the Escherichia c ...... acetyltransferase active sites
@nl
P356
P1433
P1476
Structure of the Escherichia c ...... acetyltransferase active sites
@en
P2093
S L Roderick
P304
P356
10.1021/BI002503N
P407
P577
2001-02-20T00:00:00Z