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[PMID]:27430313
[Au] Autor:Bryan MA; Hea SY; Mannering SA; Booker R
[Ad] Endereço:a Vetsouth Ltd , PO Box 12, Winton , 9741 , New Zealand.
[Ti] Título:Demonstration of non-inferiority of a novel combination intramammary antimicrobial in the treatment of clinical mastitis.
[So] Source:N Z Vet J;64(6):337-42, 2016 Nov.
[Is] ISSN:1176-0710
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: To test the non-inferiority of a novel combination intramammary product containing penicillin and cloxacillin to a reference intramammary product containing oxytetracycline, oleandomycin, neomycin and prednisolone with regard to bacteriological cure and clinical cure. METHODS: Clinical cases of mastitis were sourced from 30 spring-calving dairy farms in the Southland region of New Zealand. Affected quarters were infused three times at 24 hourly intervals with either the novel combination product containing 1 g penicillin and 200 mg cloxacillin, or a reference product containing 200 mg oxytetracycline, 100 mg oleandomycin, 100 mg neomycin and 5 mg prednisolone. Cows were enrolled when a farmer detected a case of clinical mastitis. Milk samples were collected for microbiological culture immediately before treatment (Day 0) and on Days 9, 16 and 23. Bacteriological cure was compared for 187 and 178 quarters treated with the reference and novel product, respectively, and clinical cure was compared for 235 and 223 quarters, respectively. Non-inferiority was assessed by calculating the difference in cure rates between the two products and constructing a 95% CI around the difference, using the variance inflation factor to account for herd level clustering. The non-inferiority margin was 20% for both bacteriological and clinical cure. Generalising estimating equation models were used to determine predictor variables. RESULTS: The bacteriological cure percentage, adjusted to account for herd-level clustering, was 8.5 (95% CI=-1.7-21.8)% higher for quarters treated with the novel than the reference product. The adjusted clinical cure percentage was 0.3 (95% CI=-11.2-12.0)% higher for clinical quarters treated with the novel than the reference product. Bacterial species was the only covariate for bacteriological cure (p=0.003), and quarter score at enrolment (indicating udder inflammation) was the only covariate for clinical cure (p=0.032) in the multivariable models. CONCLUSION: The novel combination product was demonstrated to be non-inferior to the reference product with regards to both bacteriological cure and clinical cure. CLINICAL RELEVANCE: Clinicians treating mastitis now have access to this novel combination intramammary product, and demonstration of its non-inferiority compared to the existing reference product will provide options for treatment approaches. The novel product contains fewer antimicrobials; which are of a narrower spectrum of activity.
[Mh] Termos MeSH primário: Anti-Infecciosos/uso terapêutico
Mastite Bovina/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Anti-Infecciosos/administração & dosagem
Bovinos
Cloxacilina/administração & dosagem
Cloxacilina/uso terapêutico
Quimioterapia Combinada/veterinária
Feminino
Injeções/veterinária
Glândulas Mamárias Animais
Neomicina/administração & dosagem
Neomicina/uso terapêutico
Oleandomicina/administração & dosagem
Oleandomicina/uso terapêutico
Oxitetraciclina/administração & dosagem
Oxitetraciclina/uso terapêutico
Penicilinas/administração & dosagem
Penicilinas/uso terapêutico
Prednisolona/administração & dosagem
Prednisolona/uso terapêutico
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Penicillins); 1404-04-2 (Neomycin); 9PHQ9Y1OLM (Prednisolone); O6X5QGC2VB (Cloxacillin); P8ZQ646136 (Oleandomycin); X20I9EN955 (Oxytetracycline)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160720
[St] Status:MEDLINE
[do] DOI:10.1080/00480169.2016.1210044


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[PMID]:26475642
[Au] Autor:Montemiglio LC; Parisi G; Scaglione A; Sciara G; Savino C; Vallone B
[Ad] Endereço:Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, P.le A. Moro 5, 00185 Rome, Italy; Department of Biochemical Sciences, "Sapienza" University of Rome, P.le A. Moro 5, 00185 Rome, Italy.
[Ti] Título:Functional analysis and crystallographic structure of clotrimazole bound OleP, a cytochrome P450 epoxidase from Streptomyces antibioticus involved in oleandomycin biosynthesis.
[So] Source:Biochim Biophys Acta;1860(3):465-75, 2016 Mar.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: OleP is a cyt P450 from Streptomyces antibioticus carrying out epoxigenation of the antibiotic oleandomycin during its biosynthesis. The timing of its reaction has not been fully clarified, doubts remain regarding its substrate and catalytic mechanism. METHODS: The crystal structure of OleP in complex with clotrimazole, an inhibitor of P450s used in therapy, was solved and the complex formation dynamics was characterized by equilibrium and kinetic binding studies and compared to ketoconazole, another azole differing for the N1-substituent. RESULTS: Clotrimazole coordinates the heme and occupies the active site. Most of the residues interacting with clotrimazole are conserved and involved in substrate binding in MycG, the P450 epoxigenase with the highest homology with OleP. Kinetic characterization of inhibitor binding revealed OleP to follow a simple bimolecular reaction, without detectable intermediates. CONCLUSIONS: Clotrimazole-bound OleP adopts an open form, held by a π-π stacking chain that fastens helices F and G and the FG loop. Affinity is affected by the interactions of the N1 substituent within the active site, given the one order of magnitude difference of the off-rate constants between clotrimazole and ketoconazole. Based on structural similarities with MycG, we propose a binding mode for both oleandomycin intermediates, that are the candidate substrates of OleP. GENERAL SIGNIFICANCE: Among P450 epoxigenases OleP is the only one that introduces an epoxide on a non-activated C­C bond. The data here presented are necessary to understand the rare chemistry carried out by OleP, to engineer it and to design more selective and potent P450-targeted drugs.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Clotrimazol/química
Sistema Enzimático do Citocromo P-450/química
Oleandomicina/biossíntese
Oxirredutases/química
Streptomyces antibioticus/enzimologia
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia
Sistema Enzimático do Citocromo P-450/fisiologia
Oxirredutases/fisiologia
Estrutura Secundária de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.- (Oxidoreductases); EC 1.- (epoxidase); G07GZ97H65 (Clotrimazole); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151018
[St] Status:MEDLINE


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[PMID]:23057817
[Au] Autor:Lu S; Zgurskaya HI
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Science Research Center, Norman, OK 73019, USA.
[Ti] Título:Role of ATP binding and hydrolysis in assembly of MacAB-TolC macrolide transporter.
[So] Source:Mol Microbiol;86(5):1132-43, 2012 Dec.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:MacB is a founding member of the Macrolide Exporter family of transporters belonging to the ATP-Binding Cassette superfamily. These proteins are broadly represented in genomes of both Gram-positive and Gram-negative bacteria and are implicated in virulence and protection against antibiotics and peptide toxins. MacB transporter functions together with MacA, a periplasmic membrane fusion protein, which stimulates MacB ATPase. In Gram-negative bacteria, MacA is believed to couple ATP hydrolysis to transport of substrates across the outer membrane through a TolC-like channel. In this study, we report a real-time analysis of concurrent ATP hydrolysis and assembly of MacAB-TolC complex. MacB binds nucleotides with a low millimolar affinity and fast on- and off-rates. In contrast, MacA-MacB complex is formed with a nanomolar affinity, which further increases in the presence of ATP. Our results strongly suggest that association between MacA and MacB is stimulated by ATP binding to MacB but remains unchanged during ATP hydrolysis cycle. We also found that the large periplasmic loop of MacB plays the major role in coupling reactions separated in two different membranes. This loop is required for MacA-dependent stimulation of MacB ATPase and at the same time, contributes to recruitment of TolC into a trans-envelope complex.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Trifosfato de Adenosina/metabolismo
Proteínas da Membrana Bacteriana Externa/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Macrolídeos/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/química
Transportadores de Cassetes de Ligação de ATP/genética
Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Proteínas da Membrana Bacteriana Externa/química
Proteínas da Membrana Bacteriana Externa/genética
Eritromicina/farmacologia
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Hidrólise
Cinética
Macrolídeos/farmacologia
Proteínas de Membrana Transportadoras/química
Proteínas de Membrana Transportadoras/genética
Testes de Sensibilidade Microbiana
Mutação
Oleandomicina/farmacologia
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Escherichia coli Proteins); 0 (MacA protein, E coli); 0 (MacB protein, E coli); 0 (Macrolides); 0 (Membrane Transport Proteins); 0 (tolC protein, E coli); 63937KV33D (Erythromycin); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121013
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.12046


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[PMID]:22377670
[Au] Autor:Bauer J; Vine M; Coric I; Bosnar M; Pasalic I; Turkalj G; Lazarevski G; Culic O; Kragol G
[Ad] Endereço:GlaxoSmithKline Research Centre Zagreb, Prilaz b. Filipovica 29, Zagreb, Croatia.
[Ti] Título:Impact of stereochemistry on the biological activity of novel oleandomycin derivatives.
[So] Source:Bioorg Med Chem;20(7):2274-81, 2012 Apr 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A set of 8-methylene-, 8-methyl-, and 8-methyl-9-dihydro-oleandomycin derivatives having different combinations of stereochemistries at positions C-8 and/or C-9 have been prepared in a chemoselective and stereoselective manner and tested in vitro for antibacterial activity and inhibition of IL-6 production. Configurations of the stereocenters at C-8 and C-9 were determined using 2D NMR techniques. We have shown that change of stereochemistry at these positions can exert a major influence on antibacterial activity as well as IL-6 inhibition, providing novel macrolide derivatives with diminished antibacterial and potent anti-inflammatory activity. In addition, the anti-inflammatory activity observed in vitro was confirmed in an in vivo model of lipopolysaccharide-induced inflammation.
[Mh] Termos MeSH primário: Antibacterianos/química
Anti-Inflamatórios/química
Oleandomicina/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Antibacterianos/síntese química
Antibacterianos/farmacologia
Anti-Inflamatórios/síntese química
Anti-Inflamatórios/farmacologia
Linhagem Celular
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Interleucina-6/metabolismo
Lipopolissacarídeos/toxicidade
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Testes de Sensibilidade Microbiana
Neutrófilos/efeitos dos fármacos
Oleandomicina/síntese química
Oleandomicina/farmacologia
Baço/citologia
Baço/efeitos dos fármacos
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Anti-Inflammatory Agents); 0 (Interleukin-6); 0 (Lipopolysaccharides); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:1207
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120302
[St] Status:MEDLINE
[do] DOI:10.1016/j.bmc.2012.02.013


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[PMID]:21696464
[Au] Autor:Modali SD; Zgurskaya HI
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA.
[Ti] Título:The periplasmic membrane proximal domain of MacA acts as a switch in stimulation of ATP hydrolysis by MacB transporter.
[So] Source:Mol Microbiol;81(4):937-51, 2011 Aug.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Escherichia coli MacAB-TolC is a tripartite macrolide efflux transporter driven by hydrolysis of ATP. In this complex, MacA is the periplasmic membrane fusion protein that stimulates the activity of MacB transporter and establishes the link with the outer membrane channel TolC. The molecular mechanism by which MacA stimulates MacB remains unknown. Here, we report that the periplasmic membrane proximal domain of MacA plays a critical role in functional MacA-MacB interactions and stimulation of MacB ATPase activity. Binding of MacA to MacB stabilizes the ATP-bound conformation of MacB, whereas interactions with both MacB and TolC affect the conformation of MacA. A single G353A substitution in the C-terminus of MacA inactivates MacAB-TolC function by changing the conformation of the membrane proximal domain of MacA and disrupting the proper assembly of the MacA-MacB complex. We propose that MacA acts in transport by promoting MacB transition into the closed ATP-bound conformation and in this respect, is similar to the periplasmic solute-binding proteins.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Trifosfato de Adenosina/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Antibacterianos/metabolismo
Antibacterianos/farmacologia
Proteínas da Membrana Bacteriana Externa/metabolismo
Eritromicina/metabolismo
Eritromicina/farmacologia
Hidrólise
Proteínas de Membrana Transportadoras/metabolismo
Testes de Sensibilidade Microbiana
Modelos Biológicos
Mutação de Sentido Incorreto
Oleandomicina/metabolismo
Oleandomicina/farmacologia
Ligação Proteica
Conformação Proteica
Mapeamento de Interação de Proteínas
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Outer Membrane Proteins); 0 (Escherichia coli Proteins); 0 (MacA protein, E coli); 0 (MacB protein, E coli); 0 (Membrane Transport Proteins); 0 (tolC protein, E coli); 63937KV33D (Erythromycin); 8L70Q75FXE (Adenosine Triphosphate); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:1112
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110624
[St] Status:MEDLINE
[do] DOI:10.1111/j.1365-2958.2011.07744.x


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[PMID]:20734590
[Au] Autor:Karou SD; Nadembega MC; Zeba B; Ilboudo DP; Ouermi D; Pignatelli S; Pietra V; Gbeassor M; De Souza C; Simpore J
[Ad] Endereço:Centre de Recherche Biomoléculaire Pietro Annigoni (CERBA), Ouagadougou, Burkina Faso. simplicekarou@hotmail.com
[Ti] Título:[Evolution of antibiotic-resistance Staphylococcus aureus in Saint Camille Medical Centre in Ouagadougou].
[Ti] Título:Evolution de la résistance de Staphylococcus aureus aux antibiotiques au Centre Médical Saint Camille de Ouagadougou..
[So] Source:Med Trop (Mars);70(3):241-4, 2010 Jun.
[Is] ISSN:0025-682X
[Cp] País de publicação:France
[La] Idioma:fre
[Ab] Resumo:BACKGROUND: Monitoring the antibiotic resistance of microorganisms in a specific geographic area can be useful in developing new approaches to first-intention antibiotherapy. OBJECTIVE: The purpose of this study was to describe the evolution of resistance of Staphylococcus aureus to antibiotics routinely used at Saint Camille Medical Centre in Ouagadougou, Burkina Faso from 1996 to 2006. METHOD: Strains of S. aureus, isolated from various pathologic sources were tested to determine their susceptibility to antibiotics. Sensitivity tests were performed in accordance with the guidelines of the Antibiogram Committee of the French Society for Microbiology (version 2007). RESULTS: During the study period, 1160 staphylococci strains were isolated including 73.45% identified as S. aureus. Susceptibility tests demonstrated a significant increase in resistance to beta-lactam antibiotics. The proportion of strains showing resistance to ampicillin reached 58.29% in 2000. Resistance to these antibiotics regressed significantly from 2000 to 2006. Resistance to pristinamycin and erythromycin showed a tendency to increase while resistance to gentamicin and oleandomycin showed no statistically significant change. CONCLUSION: This study demonstrated that S. aureus was the most common Staphylococcus genus present at the center and that it was resistant to several antibiotics. Reducing use of beta-lactam probably accounted for the significant decline in resistance to this type of antibiotic. Care should also be given to the use of other antibiotics such as pristinamycin and erythromycin since resistance appears to be increasing.
[Mh] Termos MeSH primário: Centros Médicos Acadêmicos
Antibacterianos/farmacologia
Farmacorresistência Bacteriana Múltipla
Infecções Estafilocócicas/microbiologia
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adulto
Ampicilina/farmacologia
Burkina Faso
Eritromicina/farmacologia
Feminino
Gentamicinas/farmacologia
Seres Humanos
Masculino
Testes de Sensibilidade Microbiana
Oleandomicina/farmacologia
Pristinamicina/farmacologia
Estudos Retrospectivos
Escarro/microbiologia
Infecções Estafilocócicas/tratamento farmacológico
Supuração/microbiologia
Urina/microbiologia
beta-Lactamas/farmacologia
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Gentamicins); 0 (Pristinamycin); 0 (beta-Lactams); 63937KV33D (Erythromycin); 7C782967RD (Ampicillin); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:1009
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100826
[St] Status:MEDLINE


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[PMID]:19529861
[Au] Autor:Petrovich YA; Yarema IV; Kichenko SM; Urtaev BM
[Ad] Endereço:Moscow Medical Stomatological Institute, Russia.
[Ti] Título:Study of drug transport between the blood and lymph in the predominant direction.
[So] Source:Bull Exp Biol Med;147(3):357-60, 2009 Mar.
[Is] ISSN:1573-8221
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Our method for evaluating the time course and intensity of antibiotics and other drugs transport in the predominant direction between the blood and lymph in humans promotes a more objective evaluation of drug circulation mechanisms, which is essential for determining the time of their repeated administration and route of administration. Calculation of the lymph/blood difference coefficient, based on parallel repeated measurements of the drug concentration in the lymph and blood, and of the lymph/blood coefficient provides complete data on the direction and time course of drug transport between the lymph and blood in the predominant direction.
[Mh] Termos MeSH primário: Transporte Biológico/fisiologia
Linfa/metabolismo
Preparações Farmacêuticas/sangue
[Mh] Termos MeSH secundário: Ampicilina/sangue
Ampicilina/farmacocinética
Seres Humanos
Canamicina/sangue
Canamicina/farmacocinética
Oleandomicina/sangue
Oleandomicina/farmacocinética
Peritonite/tratamento farmacológico
Tetraciclina/sangue
Tetraciclina/farmacocinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pharmaceutical Preparations); 59-01-8 (Kanamycin); 7C782967RD (Ampicillin); 8060-63-7 (sigmamycin); F8VB5M810T (Tetracycline); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:0910
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090617
[St] Status:MEDLINE


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[PMID]:18990828
[Au] Autor:Williams GJ; Thorson JS
[Ad] Endereço:Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Program, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA.
[Ti] Título:Natural product glycosyltransferases: properties and applications.
[So] Source:Adv Enzymol Relat Areas Mol Biol;76:55-119, 2009.
[Is] ISSN:0065-258X
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Glicosiltransferases/metabolismo
[Mh] Termos MeSH secundário: Aminocumarinas/metabolismo
Aminoglicosídeos/metabolismo
Antraciclinas/metabolismo
Evolução Molecular Direcionada
Desenho de Drogas
Enedi-Inos/metabolismo
Enterobactina/metabolismo
Eritromicina/metabolismo
Glicosiltransferases/química
Ivermectina/análogos & derivados
Ivermectina/metabolismo
Lactamas/metabolismo
Macrolídeos/metabolismo
Modelos Moleculares
Oleandomicina/metabolismo
Engenharia de Proteínas
Teicoplanina/metabolismo
Vancomicina/análogos & derivados
Vancomicina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Aminocoumarins); 0 (Aminoglycosides); 0 (Anthracyclines); 0 (Enediynes); 0 (Lactams); 0 (Macrolides); 0 (chloroeremomycin); 100415-25-6 (sorangicin A); 150999-05-6 (vicenistatin); 16QGD97DXG (methymycin); 28384-96-5 (Enterobactin); 61036-62-2 (Teicoplanin); 63937KV33D (Erythromycin); 6Q205EH1VU (Vancomycin); 70288-86-7 (Ivermectin); 73989-17-0 (avermectin); EC 2.4.- (Glycosyltransferases); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:0811
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:081111
[St] Status:MEDLINE


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[PMID]:18437375
[Au] Autor:Shrestha P; Oh TJ; Liou K; Sohng JK
[Ad] Endereço:Institute of Biomolecule Reconstruction (iBR), Department of Pharmaceutical Engineering, SunMoon University, Tangjeong-Myeon, Asan-Si, Chungnam, Republic of Korea.
[Ti] Título:Cytochrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin.
[So] Source:Appl Microbiol Biotechnol;79(4):555-62, 2008 Jun.
[Is] ISSN:0175-7598
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The cytochrome P450 enzyme is one of the most versatile redox proteins and it is responsible for the oxidative metabolism of a wide variety of endogenous and exogenous compounds. The cytochrome P450 gene, CYP105F2, from Streptomyces peucetius was subcloned into the pET-32a(+) vector to overexpress the protein in E. coli BL21 (DE3) pLysS. The expressed enzyme was purified by fast protein liquid chromatography with a DEAE and UNO Q column. A 3D model was constructed based on the known crystallographic structures of cytochrome P450, and comparison with PikC and MoxA signified broad substrate specificity toward structurally diverse compounds. In addition, the in vitro hydroxylation of oleandomycin by purified CYP105F2 observed in liquid chromatography/mass spectrometry and mass/mass spectrometry indicated its flexibility towards alternative polyketides for the structural diversification of the macrolide by post-polyketide synthase hydroxylation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Sistema Enzimático do Citocromo P-450/metabolismo
Expressão Gênica
Oleandomicina/metabolismo
Streptomyces/enzimologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/isolamento & purificação
Sistema Enzimático do Citocromo P-450/química
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/isolamento & purificação
Escherichia coli/genética
Escherichia coli/metabolismo
Dados de Sequência Molecular
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Especificidade por Substrato
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 9035-51-2 (Cytochrome P-450 Enzyme System); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:0809
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080426
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-008-1455-9


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[PMID]:18420146
[Au] Autor:Williams GJ; Goff RD; Zhang C; Thorson JS
[Ad] Endereço:Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Program, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705, USA.
[Ti] Título:Optimizing glycosyltransferase specificity via "hot spot" saturation mutagenesis presents a catalyst for novobiocin glycorandomization.
[So] Source:Chem Biol;15(4):393-401, 2008 Apr.
[Is] ISSN:1074-5521
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A comprehensive two-phase "hot spot" saturation mutagenesis strategy for the rapid evolution of glycosyltransferase (GT) specificity for nonnatural acceptors is described. Specifically, the application of a high-throughput screen (based on the fluorescent acceptor umbelliferone) was used to identify key amino acid hot spots that contribute to GT proficiency and/or promiscuity. Saturation mutagenesis of the corresponding hot spots facilitated the utilization of a lower-throughput screen to provide OleD prodigy capable of efficiently glycosylating the nonnatural acceptor novobiocic acid with an array of unique sugars. Incredibly, even in the absence of a high-throughput screen for novobiocic acid glycosylation, this approach rapidly led to improvements in the desired catalytic activity of several hundred-fold.
[Mh] Termos MeSH primário: Aminoácidos
Glicosiltransferases/genética
Glicosiltransferases/metabolismo
Mutagênese Sítio-Dirigida/métodos
Novobiocina/metabolismo
Oleandomicina/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Sítios de Ligação
Catálise
Evolução Molecular Direcionada
Fluorescência
Glicosilação
Glicosiltransferases/química
Cinética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 17EC19951N (Novobiocin); EC 2.4.- (Glycosyltransferases); P8ZQ646136 (Oleandomycin)
[Em] Mês de entrada:0806
[Cu] Atualização por classe:161122
[Lr] Data última revisão:
161122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080419
[St] Status:MEDLINE
[do] DOI:10.1016/j.chembiol.2008.02.017



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