Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa - Test2 - elhamkhani - TriplyDB

Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

http://www.wikidata.org/entity/Q27662400

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Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections Structure and Function of APH(4)-Ia, a Hygromycin B Resistance Enzyme Crystal Structures of Two Aminoglycoside Kinases Bound with a Eukaryotic Protein Kinase Inhibitor Aminoglycoside 2′′-Phosphotransferase IIIa (APH(2′′)-IIIa) Prefers GTP over ATP Structural Basis for Dual Nucleotide Selectivity of Aminoglycoside 2″-Phosphotransferase IVa Provides Insight on Determinants of Nucleotide Specificity of Aminoglycoside Kinases Structure-guided optimization of protein kinase inhibitors reverses aminoglycoside antibiotic resistance Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6′)-Ie-APH(2′′)-Ia Reactions of the three AmpD enzymes of Pseudomonas aeruginosa Aminoglycoside modifying enzymes.Transient kinetics of aminoglycoside phosphotransferase(3')-IIIa reveals a potential drug target in the antibiotic resistance mechanism.Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside acetyltransferase(6')-Ie/aminoglycoside phosphotransferase(2'')-Ia enzyme.Novel aminoglycoside 2''-phosphotransferase identified in a gram-negative pathogen.Aminoglycoside binding and catalysis specificity of aminoglycoside 2″-phosphotransferase IVa: A thermodynamic, structural and kinetic study Prospects for circumventing aminoglycoside kinase mediated antibiotic resistance.Emerging resistance to aminoglycosides in lactic acid bacteria of food origin-an impending menace.Effects of altering aminoglycoside structures on bacterial resistance enzyme activities.Bulky "gatekeeper" residue changes the cosubstrate specificity of aminoglycoside 2''-phosphotransferase IIa.

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

http://www.wikidata.org/entity/Q27662400

description

2010 nî lūn-bûn

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2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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type

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

@ast

Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

@en

Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Protein Science

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Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa

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Clyde A Smith

http://www.w3.org/2001/XMLSchema#string

Hilary Frase

http://www.w3.org/2001/XMLSchema#string

Marta Toth

http://www.w3.org/2001/XMLSchema#string

Nuno Tiago Antunes

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Sergei B Vakulenko

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P2860

GTP plus water mimic ATP in the active site of protein kinase CK2

Critical involvement of a carbamylated lysine in catalytic function of class D -lactamases

Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry.

The crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance

The Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside-2''-Phosphotransferase-IIa [APH(2'')-IIa] Provide Insights into Substrate Selectivity in the APH(2'') Subfamily

Structure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophila

Coot: model-building tools for molecular graphics

Refinement of macromolecular structures by the maximum-likelihood method

PHENIX: building new software for automated crystallographic structure determination

The CCP4 suite: programs for protein crystallography

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1565-76

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10.1002/PRO.437

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8

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19

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20556826

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crystal structure

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2923509

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