Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity
about
Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry.Structural Basis of APH(3')-IIIa-Mediated Resistance to N1-Substituted Aminoglycoside AntibioticsStructure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophilaStructure and Function of APH(4)-Ia, a Hygromycin B Resistance EnzymeCrystal Structures of Two Aminoglycoside Kinases Bound with a Eukaryotic Protein Kinase InhibitorInhibition of aminoglycoside-deactivating enzymes APH(3')-IIIa and AAC(6')-Ii by amphiphilic paromomycin O2''-ether analoguesStructural Basis for Dual Nucleotide Selectivity of Aminoglycoside 2″-Phosphotransferase IVa Provides Insight on Determinants of Nucleotide Specificity of Aminoglycoside KinasesMolecular mechanism of aminoglycoside antibiotic kinase APH(3')-IIIa: roles of conserved active site residuesDissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylaseKinetic mechanism of aminoglycoside phosphotransferase type IIIa. Evidence for a Theorell-Chance mechanismAminoglycosides: activity and resistance.Aminoglycoside modifying enzymes.Directed evolution of aminoglycoside phosphotransferase (3') type IIIa variants that inactivate amikacin but impose significant fitness costs.A degenerate PCR-based strategy as a means of identifying homologues of aminoglycoside and β-lactam resistance genes in the gut microbiota.Recognition of aminoglycoside antibiotics by enterococcal-staphylococcal aminoglycoside 3'-phosphotransferase type IIIa: role of substrate amino groups.Overexpression and characterization of the chromosomal aminoglycoside 6'-N-acetyltransferase from Enterococcus faecium.Influence of linker length and composition on enzymatic activity and ribosomal binding of neomycin dimers.Molecular determinants of antibiotic recognition and resistance by aminoglycoside phosphotransferase (3')-IIIa: a calorimetric and mutational analysisTransient kinetics of aminoglycoside phosphotransferase(3')-IIIa reveals a potential drug target in the antibiotic resistance mechanism.In vitro antibacterial activity of vertilmicin and its susceptibility to modifications by the recombinant AAC6'-APH2'' enzyme.Ligand promiscuity through the eyes of the aminoglycoside N3 acetyltransferase IIa.Surprising alteration of antibacterial activity of 5"-modified neomycin against resistant bacteria.Studying modification of aminoglycoside antibiotics by resistance-causing enzymes via microarray.Novel thermostable antibiotic resistance enzymes from the Atlantis II Deep Red Sea brine pool.Purification and characterization of aminoglycoside phosphotransferase APH(6)-Id, a streptomycin-inactivating enzyme.Prospects for circumventing aminoglycoside kinase mediated antibiotic resistance.Characterization of AziR, a resistance protein of the DNA cross-linking agent azinomycin B.Functional and kinetic analysis of the phosphotransferase CapP conferring selective self-resistance to capuramycin antibiotics.Nucleotide selectivity of antibiotic kinases.Spectinomycin kinase from Legionella pneumophila. Characterization of substrate specificity and identification of catalytically important residues.Inhibition of aminoglycoside antibiotic resistance enzymes by protein kinase inhibitors.Overexpression and initial characterization of the chromosomal aminoglycoside 3'-O-phosphotransferase APH(3')-IIb from Pseudomonas aeruginosa.Aminoglycoside 2''-phosphotransferase type IIIa from Enterococcus.A second-site suppressor strategy for chemical genetic analysis of diverse protein kinases.Self-Resistance During Muraymycin Biosynthesis: A Complementary Nucleotidyltransferase and Phosphotransferase with Identical Modification Sites and Distinct Temporal Order.Simultaneous inhibition assay for human and microbial kinases via MALDI-MS/MS.Enzymatic analysis of a thermostabilized mutant of an Escherichia coli hygromycin B phosphotransferase.Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation.Nucleoside triphosphate cosubstrates control the substrate profile and efficiency of aminoglycoside 3'--phosphotransferase type IIa
P2860
Q27638972-C7E30CDC-A905-4348-99CD-6ADC2DEFAA67Q27655445-C641303A-B9F6-46CE-A9B9-28184826DB10Q27659071-98EAA01A-71CD-4509-B4D9-D1E1BA500705Q27665944-4807E8BF-61EF-4403-A408-B8F3A7D8AF8AQ27667856-1E785B5E-08F0-4797-A930-9FF9E71BF03CQ27673672-46C1C0D0-7544-4DAD-81DB-17455793F4A5Q27677520-D3EED9EE-8F2B-45EA-8E1A-2F5B1297A18DQ28208636-9827ACC7-DD78-4562-9408-38837A7BAE44Q28235383-0B7C72F2-01B8-4FC4-A154-E860DB7C81D4Q28289501-A4A7AA10-2BA7-406A-8032-4A1537F04995Q33548221-BA74273F-9C94-48F6-80DD-EF7CBA2F3200Q34354185-E9721708-E35C-4860-9E53-B3AE829E2822Q35034759-9C691FE0-5892-4639-A9E8-223590D4CC62Q35086954-4ACC6C42-9A77-4CBD-B8C5-F24FFCE5D72CQ35129429-5548B29F-4916-4960-AE99-B9B1EDF10644Q35135819-E9F2BCF9-E84E-4C7E-9CC0-B709AB055DFAQ35746019-B7D75F40-5980-4157-8806-0566C15AB44CQ36088314-17974573-F8DC-44F4-AE51-56C1B0D9CD7AQ36434917-01EB13C7-B5B0-43A6-9AF5-E0CD717C8B65Q36949450-B45552A8-387B-4D28-BF88-FC3E6222CD84Q37034579-0DA89772-42B7-436C-872F-FD7D816443B9Q37147220-B9BD81D7-3B1E-4DF4-8DDC-F60BD7C242CBQ37257100-6AF531E4-95D2-4968-9BD9-31D175151C85Q37610278-1EA6A6B5-9BC2-4C2F-A9F9-2F40FA02AE2CQ37618069-1FF886A3-F44C-4DDD-980D-1551C3106652Q38117380-91A0A33E-D16C-4F05-AABD-0407E7A5678AQ39726494-ED9FE761-3D8F-4815-B0BE-50F9FE03D66BQ40105078-003C415D-D7A7-436D-86BA-169F292B4667Q40337157-755B47CC-FE75-472A-B296-63F991F8F6D2Q40855507-8BF2021D-AC4B-4541-9F3C-5C9B5831092FQ40881651-E2DDFC08-993D-4603-9ED2-4B17FE80C306Q42956760-1B6007E3-777F-4C18-A496-C09BDAEC4A9BQ46804930-E0297EA8-3B95-4F85-9005-3170AF3692A1Q51458365-ACA114FF-129C-4236-BDB0-3CC4865EA50DQ53686612-0562711A-7077-47A1-89CE-FEAA68409CE7Q54381127-FB1DCD6B-8FEB-4AE0-BA1B-12498883B900Q54417060-8B24CC18-A67D-489E-A25E-A57BA85364E9Q54436749-51A82BA5-A5AC-48A5-8A38-0E0AE94EB475Q57814963-32C5A6CB-DF7B-4697-A9D1-C321DFD67CA6
P2860
Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@ast
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@en
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@nl
type
label
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@ast
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@en
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@nl
prefLabel
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@ast
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@en
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@nl
P356
P1433
P1476
Broad spectrum aminoglycoside ...... ion, and substrate specificity
@en
P2093
P R Thompson
P304
P356
10.1021/BI00188A024
P407
P577
1994-06-07T00:00:00Z