About: Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance

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About: Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance Goto Sponge Distinct Permalink

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scientific article published on 01 May 2001

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) bài báo khoa học (vi) наукова стаття, опублікована в травні 2001 (uk) article scientifique publié en 2001 (fr) im Mai 2001 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en mayu de 2001 (ast) scientific article published on 01 May 2001 (en)
publication date	wds:Q73852591-05CBC285-7A8D-47D5-A0C7-C09B1F07B523
publication date	2001-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73852591-4B6610B6-2796-4270-B1C6-D4849CB7A837
language of work or name	English
cites work	wds:Q73852591-0148DC44-5C20-4327-B3C6-4D9FA4363F39 wds:Q73852591-06BA764B-1CF1-4181-96AF-257503153707 wds:Q73852591-0B8B8B51-108A-4AE4-B8C2-5066CBBB05E6 wds:Q73852591-0DF7F0F7-2AE5-4780-AC6E-CD1D3F0ED8A2 wds:Q73852591-1104681C-95D7-4AD0-9564-6D12BF93B6E4 wds:Q73852591-15AF9C3C-073F-4E99-95C7-6372F6A488B9 wds:Q73852591-1C1677BB-0C1B-4232-B52A-05B9A3AD7DED wds:Q73852591-1E82038B-DBED-4A2C-8A00-B41EF71501DB wds:Q73852591-2A054955-A691-4A2E-BC59-B87B005B82DB wds:Q73852591-2C2A5C4E-D736-4C08-8FDA-BC33B17EC0C7 wds:Q73852591-2CEC9C92-26C6-4890-BFBD-AAF0C1EA70F4 wds:Q73852591-30D19166-6538-44B6-BA54-2A2EA7B1810D wds:Q73852591-3A53EB29-C6A5-49E9-8759-941CD0954657 wds:Q73852591-44D6A039-AA28-4E82-A8F9-D10CCD02D299 wds:Q73852591-4F51B1D7-FBE7-45F6-B447-60E0BF056C4E wds:Q73852591-55D82A68-173B-41C1-8B0C-0F7C2D87B72A wds:Q73852591-5A1ED68A-6FF0-49D2-A390-B922ED008F87 wds:Q73852591-5F135265-273E-463D-9A42-70F545B85531 wds:Q73852591-5F2A8F6A-5EE7-4C55-8A0B-267CBBCD4D20 wds:Q73852591-623D7040-CF11-4238-B53D-A5696A803DCF wds:Q73852591-68F001C1-7FA8-445E-8DA6-F84CEC6E24A1 wds:Q73852591-6D0E6254-E03B-40EA-8CC4-D8316750069B wds:Q73852591-72544E7F-32FA-4F94-904F-A6F9C277648F wds:Q73852591-7F90496E-043D-4125-8D1A-21D70735FCA1 wds:Q73852591-87959B6F-7324-43C8-B8F6-EABAE218DDF3 wds:Q73852591-8EA9BE38-7BFE-4472-8277-8E446FCACE26 wds:Q73852591-A278353E-4A6B-4F6D-B0AA-0825EF7FBAED wds:Q73852591-A33293FD-FB92-496E-9778-96E84E61F138 wds:Q73852591-AAC62A21-5337-466C-BAE5-F55C2FD813C6 wds:Q73852591-AB3C83E6-2B23-4617-9F01-F781DF102558 wds:Q73852591-B18D57B7-01C8-4552-A9AE-2A20D560E89B wds:Q73852591-D51A5D2A-D0E1-4ECC-A7D0-6B60AE8FFA12 wds:Q73852591-E1890A01-B960-46FA-95CC-A5766A04BA4C wds:Q73852591-E19B92A2-EE4A-4B2F-A351-5D84A7770D12 wds:Q73852591-F0859D22-6BFE-4F8F-945A-3185704C25B6 wds:Q73852591-F495BB52-335E-43B2-A30F-976EA9F84EED
cites work	The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibiotics A functional classification scheme for beta-lactamases and its correlation with molecular structure The structure of β-lactamases Amino acid sequence determinants of beta-lactamase structure and activity Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme beta-Lactamases in laboratory and clinical resistance SHV-7, a novel cefotaxime-hydrolyzing beta-lactamase, identified in Escherichia coli isolates from hospitalized nursing home patients Effects of Asp-179 mutations in TEMpUC19 beta-lactamase on susceptibility to beta-lactams Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamase High-level expression of chromosomally encoded SHV-1 beta-lactamase and an outer membrane protein change confer resistance to ceftazidime and piperacillin-tazobactam in a clinical isolate of Klebsiella pneumoniae Emergence of an inhibitor-resistant beta-lactamase (SHV-10) derived from an SHV-5 variant. The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family A standard numbering scheme for the class A beta-lactamases TEM beta-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis. Structure of the SHV-1 beta-lactamase Multiple substitutions at position 104 of beta-lactamase TEM-1: assessing the role of this residue in substrate specificity. Clinical inhibitor-resistant mutants of the beta-lactamase TEM-1 at amino-acid position 69. Kinetic analysis and molecular modelling Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure Evolution and dissemination of beta-lactamases accelerated by generations of beta-lactam antibiotics Catalytic mechanism of active-site serine beta-lactamases: role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly triad Catalytic properties of class A beta-lactamases: efficiency and diversity Site-directed mutagenesis of .beta.-lactamase leading to accumulation of a catalytic intermediate Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of beta-lactamases Effects on substrate profile by mutational substitutions at positions 164 and 179 of the class A TEM(pUC19) beta-lactamase from Escherichia coli. Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by beta-lactamase TEM-1 and the G238S mutant. Substitution of lysine at position 104 or 240 of TEM-1pTZ18R beta-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam. Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of beta-lactamase. Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution A catalytically-impaired class A beta-lactamase: 2 A crystal structure and kinetics of the Bacillus licheniformis E166A mutant Interactions of new plasmid-mediated beta-lactamases with third-generation cephalosporins Critical hydrogen bonding by serine 235 for cephalosporinase activity of TEM-1 beta-lactamase Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase. In-vitro antimicrobial activity of HMR 3004 (RU 64004) against erythromycin A-sensitive and -resistant Corynebacterium spp. isolated from clinical specimens OHIO-1 beta-lactamase mutants: the Arg244Ser mutant and resistance to beta-lactams and beta-lactamase inhibitors Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1 Aspartic acid for asparagine substitution at position 276 reduces susceptibility to mechanism-based inhibitors in SHV-1 and SHV-5 beta-lactamases
author name string	wds:Q73852591-98A1E9D7-02D6-4795-A7DB-303385627E25 wds:Q73852591-E12AA2BD-27CC-47FD-A5E1-822FBBD8EDD5 wds:Q73852591-F597B806-D0F5-4727-8BDF-16709D2F9876
author name string	R A Bonomo A M Hujer K M Hujer
rdfs:label	Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (en) Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (nl)
skos:prefLabel	Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (en) Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (nl)
name	Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (en) Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (nl)
title	wds:Q73852591-4F4249CB-31AA-4188-80D7-49AE65543DA5
title	Mutagenesis of amino acid residues in the SHV-1 beta-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance (en)
page(s)	wds:Q73852591-0E7580D2-0B33-402D-85AB-49D3DFFB6587
page(s)	37-50

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