Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton
about
Structure-Based Inhibitors Exhibit Differential Activities againstHelicobacter pyloriandEscherichia coliUndecaprenyl Pyrophosphate SynthasesApplying Molecular Dynamics Simulations to Identify Rarely Sampled Ligand-bound Conformational States of Undecaprenyl Pyrophosphate Synthase, an Antibacterial TargetDeciphering the metabolism of undecaprenyl-phosphate: the bacterial cell-wall unit carrier at the membrane frontierProposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.Species differences in alternative substrate utilization by the antibacterial target undecaprenyl pyrophosphate synthase.Tuning the production of variable length, fluorescent polyisoprenoids using surfactant-controlled enzymatic synthesis.Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies.Undecaprenyl diphosphate synthase, a cis-prenyltransferase synthesizing lipid carrier for bacterial cell wall biosynthesis.cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases.Biophysical investigation of the mode of inhibition of tetramic acids, the allosteric inhibitors of undecaprenyl pyrophosphate synthase.Discovery and structural characterization of an allosteric inhibitor of bacterial cis-prenyltransferase.Chemoenzymatic synthesis of an isoprenoid phosphate tool for the analysis of complex bacterial oligosaccharide biosynthesis.Crystallization and preliminary X-ray diffraction analysis of cyclolavandulyl diphosphate synthase, a new member of the cis-isoprenyl diphosphate synthase superfamily.Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase.Dependence of the product chain-length on detergents for long-chain E-polyprenyl diphosphate synthases.Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli.Triton X-100 inhibition of yeast plasma membrane associated NADH-dependent redox activities.Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase.The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme.A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity.
P2860
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P2860
Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@ast
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@en
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@nl
type
label
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@ast
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@en
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@nl
prefLabel
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@ast
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@en
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@nl
P2860
P921
P356
P1476
Catalytic mechanism revealed b ...... sulfate, magnesium, and triton
@en
P2093
Po-Huang Liang
Sing-Yang Chang
P2860
P304
P356
10.1074/JBC.M302687200
P407
P577
2003-08-01T00:00:00Z