Nucleoside triphosphate cosubstrates control the substrate profile and efficiency of aminoglycoside 3'--phosphotransferase type IIa

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Nucleoside triphosphate cosubstrates control the substrate profile and efficiency of aminoglycoside 3'--phosphotransferase type IIa

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http://www.wikidata.org/entity/Q57814963

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im August 2018 veröffentlichter wissenschaftlicher Artikel

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scientific article published on 16 July 2018

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wetenschappelijk artikel

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наукова стаття, опублікована в серпні 2018

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name

Nucleoside triphosphate cosubs ...... '--phosphotransferase type IIa

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Nucleoside triphosphate cosubs ...... '--phosphotransferase type IIa

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type

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label

Nucleoside triphosphate cosubs ...... '--phosphotransferase type IIa

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Nucleoside triphosphate cosubs ...... '--phosphotransferase type IIa

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prefLabel

Nucleoside triphosphate cosubs ...... '--phosphotransferase type IIa

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Nucleoside triphosphate cosubs ...... '--phosphotransferase type IIa

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P1476

Nucleoside triphosphate cosubs ...... -O-phosphotransferase type IIa

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P2093

Matthew S Gentry

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Selina Y L Holbrook

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Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections

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

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

Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity

Catalytic mechanism of enterococcal kanamycin kinase (APH(3')-IIIa): viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism

Kinetic mechanism of aminoglycoside phosphotransferase type IIIa. Evidence for a Theorell-Chance mechanism

Aminoglycoside phosphotransferases: proteins, structure, and mechanism

A mutant neomycin phosphotransferase II gene reduces the resistance of transformants to antibiotic selection pressure

P304

1332-1339

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P31

scholarly article

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10.1039/C8MD00234G

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English

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P478

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Sylvie Garneau-Tsodikova

Oleg V Tsodikov

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2018-07-16T00:00:00Z

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30151088

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P932

6097461

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