Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies

Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies

Item
http://www.wikidata.org/entity/Q27670438
Insights into Phosphate Cooperativity and Influence of Substrate Modifications on Binding and Catalysis of Hexameric Purine Nucleoside PhosphorylasesStructural basis of the substrate specificity ofBacillus cereusadenosine phosphorylaseNew phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin AHigh-syn conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis MR-1 uridine phosphorylase in the free form and in complex with uridineMolecular replacement with a large number of molecules in the asymmetric unitSolution structures of purine base analogues 9-deazaguanine and 9-deazahypoxanthine.Purine nucleoside phosphorylase targeted by annexin v to breast cancer vasculature for enzyme prodrug therapy.Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase.New Insights into Active Site Conformation Dynamics of E. coli PNP Revealed by Combined H/D Exchange Approach and Molecular Dynamics Simulations.Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides.Unique substrate specificity of purine nucleoside phosphorylases from Thermus thermophilus.Site-Selective Ribosylation of Fluorescent Nucleobase Analogs Using Purine-Nucleoside Phosphorylase as a Catalyst: Effects of Point Mutations.Recognition of Artificial Nucleobases by E. coli Purine Nucleoside Phosphorylase versus its Ser90Ala Mutant in the Synthesis of Base-Modified Nucleosides.Enzymatic synthesis of highly fluorescent 8-azapurine ribosides using a purine nucleoside phosphorylase reverse reaction: variable ribosylation sites.Crystallographic snapshots of ligand binding to hexameric purine nucleoside phosphorylase and kinetic studies give insight into the mechanism of catalysis
P2860

Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies

Item
http://www.wikidata.org/entity/Q27670438
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Validation of the catalytic me ...... structural and kinetic studies
@ast
Validation of the catalytic me ...... structural and kinetic studies
@en
Validation of the catalytic me ...... structural and kinetic studies
@nl
type
label
Validation of the catalytic me ...... structural and kinetic studies
@ast
Validation of the catalytic me ...... structural and kinetic studies
@en
Validation of the catalytic me ...... structural and kinetic studies
@nl
prefLabel
Validation of the catalytic me ...... structural and kinetic studies
@ast
Validation of the catalytic me ...... structural and kinetic studies
@en
Validation of the catalytic me ...... structural and kinetic studies
@nl
P1433
P1476
P2093
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P478
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P356
P1433
P1476
Validation of the catalytic me ...... structural and kinetic studies
@en
P2093
P304
P31
P356
10.1016/J.BIOCHI.2011.05.030
P433
P478
P577
P698