Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Relationship between the two activities.

Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Relationship between the two activities.

Item
http://www.wikidata.org/entity/Q54495323
Mechanistic and Structural Analysis of Aminoglycoside N -Acetyltransferase AAC(6′)-Ib and Its Bifunctional, Fluoroquinolone-Active AAC(6′)-Ib-cr Variant † ‡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'') SubfamilyCrystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVaKinetic mechanism of aminoglycoside phosphotransferase type IIIa. Evidence for a Theorell-Chance mechanismA random sequential mechanism of aminoglycoside acetylation by Mycobacterium tuberculosis Eis proteinStructure of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia revealed by crystallographic and small-angle X-ray scattering analysis.Aminoglycoside multiacetylating activity of the enhanced intracellular survival protein from Mycobacterium smegmatis and its inhibition.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.Comparison of the gentamicin resistance transposon Tn5281 with regions encoding gentamicin resistance in Enterococcus faecalis isolates from diverse geographic locations.Antimicrobial resistance of Staphylococcus aureus: genetic basis.Understanding and overcoming aminoglycoside resistance caused by N-6'-acetyltransferase.The molecular basis of the expansive substrate specificity of the antibiotic resistance enzyme aminoglycoside acetyltransferase-6'-aminoglycoside phosphotransferase-2". The role of ASP-99 as an active site base important for acetyl transfer.Mobilization of the gentamicin resistance gene in Enterococcus faecalis.Characterization of the gentamicin resistance transposon Tn5281 from Enterococcus faecalis and comparison to staphylococcal transposons Tn4001 and Tn4031.Small-angle X-ray scattering analysis of the bifunctional antibiotic resistance enzyme aminoglycoside (6') acetyltransferase-ie/aminoglycoside (2'') phosphotransferase-ia reveals a rigid solution structure.Aminoglycoside 2''-phosphotransferase type IIIa from Enterococcus.
P2860

Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Relationship between the two activities.

Item
http://www.wikidata.org/entity/Q54495323
description
1983 nî lūn-bûn
@nan
1983年の論文
@ja
1983年学术文章
@wuu
1983年学术文章
@zh-cn
1983年学术文章
@zh-hans
1983年学术文章
@zh-my
1983年学术文章
@zh-sg
1983年學術文章
@yue
1983年學術文章
@zh
1983年學術文章
@zh-hant
name
Kinetic studies of aminoglycos ...... ip between the two activities.
@en
Kinetic studies of aminoglycos ...... ip between the two activities.
@nl
type
label
Kinetic studies of aminoglycos ...... ip between the two activities.
@en
Kinetic studies of aminoglycos ...... ip between the two activities.
@nl
prefLabel
Kinetic studies of aminoglycos ...... ip between the two activities.
@en
Kinetic studies of aminoglycos ...... ip between the two activities.
@nl
P1433
P1476
P2093
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P5875
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P1433
P1476
Kinetic studies of aminoglycos ...... ip between the two activities.
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P2093
P2860
P304
P31
P356
10.1111/J.1432-1033.1983.TB07494.X
P407
P433
P478
P577
P5875
P698