Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2''-phosphotransferases.
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ABC1K atypical kinases in plants: filling the organellar kinase voidThe 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'') SubfamilyStructure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophilaCrystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVaStructure and Function of APH(4)-Ia, a Hygromycin B Resistance EnzymeAminoglycoside 2′′-Phosphotransferase IIIa (APH(2′′)-IIIa) Prefers GTP over ATPStructural Basis for Dual Nucleotide Selectivity of Aminoglycoside 2″-Phosphotransferase IVa Provides Insight on Determinants of Nucleotide Specificity of Aminoglycoside KinasesStructure-guided optimization of protein kinase inhibitors reverses aminoglycoside antibiotic resistanceStructure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6′)-Ie-APH(2′′)-IaPurification, crystallization and preliminary X-ray analysis of Enterococcus casseliflavus aminoglycoside-2''-phosphotransferase-IVa.Mutant APH(2'')-IIa enzymes with increased activity against amikacin and isepamicinStructure of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia revealed by crystallographic and small-angle X-ray scattering analysis.Aminoglycoside modifying enzymes.Characterization of ribosomal binding and antibacterial activities using two orthogonal high-throughput screensThe Biosynthesis of Capuramycin-type Antibiotics: IDENTIFICATION OF THE A-102395 BIOSYNTHETIC GENE CLUSTER, MECHANISM OF SELF-RESISTANCE, AND FORMATION OF URIDINE-5'-CARBOXAMIDE.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 studyProspects for circumventing aminoglycoside kinase mediated antibiotic resistance.Nucleotide selectivity of antibiotic kinases.Effects of altering aminoglycoside structures on bacterial resistance enzyme activities.Bulky "gatekeeper" residue changes the cosubstrate specificity of aminoglycoside 2''-phosphotransferase IIa.Multiple keys for a single lock: the unusual structural plasticity of the nucleotidyltransferase (4')/kanamycin complex.Whole-Genome Sequence Analysis of Multidrug-Resistant Campylobacter Isolates: a Focus on Aminoglycoside Resistance Determinants
P2860
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P2860
Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2''-phosphotransferases.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Source of phosphate in the enz ...... oside 2''-phosphotransferases.
@en
type
label
Source of phosphate in the enz ...... oside 2''-phosphotransferases.
@en
prefLabel
Source of phosphate in the enz ...... oside 2''-phosphotransferases.
@en
P2093
P2860
P356
P1476
Source of phosphate in the enz ...... coside 2''-phosphotransferases
@en
P2093
Marta Toth
Sergei B Vakulenko
Shahriar Mobashery
P2860
P304
P356
10.1074/JBC.M808148200
P407
P577
2009-01-21T00:00:00Z