Base de dados : MEDLINE
Pesquisa : B01.300.107.320.215 [Categoria DeCS]
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[PMID]:28333449
[Au] Autor:Li G; Kusari S; Golz C; Laatsch H; Strohmann C; Spiteller M
[Ad] Endereço:Institute of Environmental Research (INFU), Department of Chemistry and Chemical Biology, Chair of Environmental Chemistry and Analytical Chemistry, TU Dortmund , Otto-Hahn-Straße 6, 44221 Dortmund, Germany.
[Ti] Título:Epigenetic Modulation of Endophytic Eupenicillium sp. LG41 by a Histone Deacetylase Inhibitor for Production of Decalin-Containing Compounds.
[So] Source:J Nat Prod;80(4):983-988, 2017 Apr 28.
[Is] ISSN:1520-6025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An endophytic fungus, Eupenicillium sp. LG41, isolated from the Chinese medicinal plant Xanthium sibiricum, was subjected to epigenetic modulation using an NAD -dependent histone deacetylase (HDAC) inhibitor, nicotinamide. Epigenetic stimulation of the endophyte led to enhanced production of two new decalin-containing compounds, eupenicinicols C and D (3 and 4), along with two biosynthetically related known compounds, eujavanicol A (1) and eupenicinicol A (2). The structures and stereochemistry of the new compounds were elucidated by extensive spectroscopic analysis using LC-HRMS, NMR, optical rotation, and ECD calculations, as well as single-crystal X-ray diffraction. Compounds 3 and 4 exist in chemical equilibrium with two and three cis/trans isomers, respectively, as revealed by LC-MS analysis. Compound 4 was active against Staphylococcus aureus with an MIC of 0.1 µg/mL and demonstrated marked cytotoxicity against the human acute monocytic leukemia cell line (THP-1). We have shown that the HDAC inhibitor, nicotinamide, enhanced the production of compounds 3 and 4 by endophytic Eupenicillium sp. LG41, facilitating their isolation, structure elucidation, and evaluation of their biological activities.
[Mh] Termos MeSH primário: Eupenicillium/química
Inibidores de Histona Desacetilases/farmacologia
Naftalenos/química
Xanthium/microbiologia
[Mh] Termos MeSH secundário: Antibacterianos/química
Bacillus subtilis/efeitos dos fármacos
Cristalografia por Raios X
Medicamentos de Ervas Chinesas/química
Endófitos/química
Seres Humanos
Testes de Sensibilidade Microbiana
Estrutura Molecular
Naftalenos/isolamento & purificação
Naftalenos/farmacologia
Ressonância Magnética Nuclear Biomolecular
Penicillium/química
Staphylococcus aureus/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Drugs, Chinese Herbal); 0 (Histone Deacetylase Inhibitors); 0 (Naphthalenes); 0 (eujavanicol A); 0 (eupenicinicol A); 88451Q4XYF (decalin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jnatprod.6b00997


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[PMID]:27329796
[Au] Autor:Yasuno Y; Hamada M; Yoshida Y; Shimamoto K; Shigeri Y; Akizawa T; Konishi M; Ohfune Y; Shinada T
[Ad] Endereço:Graduate School of Science, Osaka City University, 3-3-138, Sugimoto, Sumiyoshi, Osaka 558-8585, Japan.
[Ti] Título:Structure-activity relationship study at C9 position of kaitocephalin.
[So] Source:Bioorg Med Chem Lett;26(15):3543-6, 2016 08 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Kaitocephalin (KCP) isolated from Eupenicillium shearii PF1191 is an unusual amino acid natural product in which serine, proline, and alanine moieties are liked with carbon-carbon bonds. KCP exhibits potent and selective binding affinity for one of the ionotropic glutamate receptor subtypes, NMDA receptors (Ki=7.8nM). In this study, new structure-activity relationship studies at C9 of KCP were implemented. Eleven new KCP analogs with different substituents at C9 were prepared and employed for binding affinity tests using native ionotropic glutamate receptors. Replacement of the 3,5-dichloro-4-hydroxybenzoyl group of KCP with a 3-phenylpropionyl group resulted in significant loss of binding affinity for NMDARs (Ki=1300nM), indicating an indispensable role of the aromatic ring of KCP in the potent and selective binding to NMDARs. Other analogs showed potent binding affinity in a range of 11-270nM. These findings would directly link to develop useful chemical tools toward imaging and labeling of NMDARs.
[Mh] Termos MeSH primário: Pirróis/farmacologia
Receptores de N-Metil-D-Aspartato/antagonistas & inibidores
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Eupenicillium/química
Seres Humanos
Estrutura Molecular
Pirróis/química
Pirróis/isolamento & purificação
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Pyrroles); 0 (Receptors, N-Methyl-D-Aspartate); 9B96C79PCS (kaitocephalin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160623
[St] Status:MEDLINE


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[PMID]:27171788
[Au] Autor:Long L; Ding D; Han Z; Zhao H; Lin Q; Ding S
[Ad] Endereço:College of Chemical Engineering, Nanjing Forestry University, Nanjing, China.
[Ti] Título:Thermotolerant hemicellulolytic and cellulolytic enzymes from Eupenicillium parvum 4-14 display high efficiency upon release of ferulic acid from wheat bran.
[So] Source:J Appl Microbiol;121(2):422-34, 2016 Aug.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: To characterize the hemicellulolytic and cellulolytic enzymes from novel fungi, and evaluate the potential of novel enzyme system in releasing ferulic acid (FA) from biomass resource. METHODS AND RESULTS: A hemicellulolytic and cellulolytic enzyme-producing fungus 4-14 was isolated from soil by Congo red staining method, and identified as Eupenicillium parvum based on the morphologic and molecular phylogenetic analysis. The optimum temperature of fungal growth was 37°C. Hemicellulolytic and cellulolytic enzymes were produced by this fungus in solid-state fermentation (SSF), and their maximum activities were 554, 385, 218, 2·62 and 5·25 U g(-1) for CMCase, xylanase, ß-glucosidase, FPase and FAE respectively. These enzymes displayed the best catalytic ability at low pH values (pH 4·5-5·0). The optimum temperatures were 70°C, 70°C, 75°C and 55°C for CMCase, ß-glucosidase, xylanase and FAE respectively. CMCase, xylanase and FAE were stable at different pHs or high temperature (60°C). Enzymatic hydrolysis experiment indicated that the maximum (76·8 ± 4)% of total alkali-extractable FA was released from de-starched wheat bran by the fungal enzyme system. CONCLUSIONS: High activities of thermotolerant CMCase, ß-glucosidase, xylanase and FAE were produced by the newly isolated fungus E. parvum 4-14 in SSF. The fungal enzyme system displayed high efficiency at releasing FA from wheat bran. SIGNIFICANCE AND IMPACT OF THE STUDY: This study provides a new fungal strain for researches of novel hemicellulolytic and cellulolytic enzymes and will improve the bioconversion and utilization of agricultural by-products.
[Mh] Termos MeSH primário: Celulase/metabolismo
Ácidos Cumáricos/análise
Fibras na Dieta/metabolismo
Eupenicillium/enzimologia
Proteínas Fúngicas/metabolismo
beta-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Celulase/química
Celulase/genética
Ácidos Cumáricos/metabolismo
Fibras na Dieta/análise
Eupenicillium/química
Eupenicillium/classificação
Eupenicillium/genética
Fermentação
Proteínas Fúngicas/química
Hidrólise
Filogenia
Temperatura Ambiente
beta-Glucosidase/química
beta-Glucosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coumaric Acids); 0 (Dietary Fiber); 0 (Fungal Proteins); AVM951ZWST (ferulic acid); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.4 (Cellulase); EC 3.2.1.4 (carboxymethylcellulase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160513
[St] Status:MEDLINE
[do] DOI:10.1111/jam.13177


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[PMID]:26660454
[Au] Autor:Yasuno Y; Hamada M; Kawasaki M; Shimamoto K; Shigeri Y; Akizawa T; Konishi M; Ohfune Y; Shinada T
[Ad] Endereço:Graduate School of Science, Osaka City University, 3-3-138, Sugimoto, Sumiyoshi, Osaka 558-8585, Japan. shinada@sci.osaka-cu.ac.jp.
[Ti] Título:(7S)-Kaitocephalin as a potent NMDA receptor selective ligand.
[So] Source:Org Biomol Chem;14(4):1206-10, 2016 Jan 28.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A structure-activity relationship (SAR) study of kaitocephalin (KCP), known to be a potent naturally occurring NMDA receptor ligand, was performed. This study led us to the discovery of (7S)-kaitocephalin as a highly selective NMDA receptor ligand. It displayed a 22-fold higher degree of selectivity for the NMDA receptor over KCP, though the binding affinity of (7S)-KCP [Ki = 29 nM] was 3.7-fold less potent than that of KCP [Ki = 7.8 nM].
[Mh] Termos MeSH primário: Pirróis/farmacologia
Receptores de N-Metil-D-Aspartato/antagonistas & inibidores
Receptores de N-Metil-D-Aspartato/metabolismo
[Mh] Termos MeSH secundário: Animais
Relação Dose-Resposta a Droga
Eupenicillium/química
Ligantes
Conformação Molecular
Pirróis/síntese química
Pirróis/química
Ratos
Estereoisomerismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ligands); 0 (Pyrroles); 0 (Receptors, N-Methyl-D-Aspartate); 9B96C79PCS (kaitocephalin)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1039/c5ob02301g


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[PMID]:26397819
[Au] Autor:Lu Z; Li H; Bian M; Li A
[Ad] Endereço:State Key Laboratory of Bioorganic and Natural Products Chemistry, Collaborative Innovation Center of Chemistry for Life Sciences, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences , 345 Lingling Road, Shanghai 200032, China.
[Ti] Título:Total Synthesis of Epoxyeujindole A.
[So] Source:J Am Chem Soc;137(43):13764-7, 2015 Nov 04.
[Is] ISSN:1520-5126
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The total synthesis of epoxyeujindole A, a structurally unusual indole diterpenoid isolated from Eupenicillium javanicum, has been accomplished for the first time. The synthesis features a late-stage cationic cyclization strategy, which took advantage of an electron-rich olefinic substrate. The CDE ring system was assembled via an enantioselective conjugate addition/alkylation, a Luche cyclization, and a Nozaki-Hiyama-Kishi reaction. The heavily substituted A ring was constructed through a Suzuki-Miyaura coupling and a cationic cyclization, and the bridged fused B ring was formed through a Prins reaction.
[Mh] Termos MeSH primário: Diterpenos/síntese química
Eupenicillium/química
[Mh] Termos MeSH secundário: Ciclização
Diterpenos/química
Modelos Moleculares
Conformação Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Diterpenes); 0 (epoxyeujindole A)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:151104
[Lr] Data última revisão:
151104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150924
[St] Status:MEDLINE
[do] DOI:10.1021/jacs.5b09198


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[PMID]:25849495
[Au] Autor:Gan W; Gao F; Xing K; Jia M; Liu H; Gong W
[Ad] Endereço:Key Laboratory of RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
[Ti] Título:Structural basis of the substrate specificity of the FPOD/FAOD family revealed by fructosyl peptide oxidase from Eupenicillium terrenum.
[So] Source:Acta Crystallogr F Struct Biol Commun;71(Pt 4):381-7, 2015 Apr.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The FAOD/FPOD family of proteins has the potential to be useful for the longterm detection of blood glucose levels in diabetes patients. A bottleneck for this application is to find or engineer a FAOD/FPOD family enzyme that is specifically active towards α-fructosyl peptides but is inactive towards other types of glycated peptides. Here, the crystal structure of fructosyl peptide oxidase from Eupenicillium terrenum (EtFPOX) is reported at 1.9 Šresolution. In contrast to the previously reported structure of amadoriase II, EtFPOX has an open substrate entrance to accommodate the large peptide substrate. The functions of residues critical for substrate selection are discussed based on structure comparison and sequence alignment. This study reveals the first structural details of group I FPODs that prefer α-fructosyl substrates and could provide significant useful information for uncovering the mechanism of substrate specificity of FAOD/FPODs and guidance towards future enzyme engineering for diagnostic purposes.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/química
Aminoácido Oxirredutases/metabolismo
Eupenicillium/enzimologia
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/genética
Sequência de Aminoácidos
Seres Humanos
Dados de Sequência Molecular
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Especificidade por Substrato/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.4.- (Amino Acid Oxidoreductases); EC 1.5.3.- (amadoriase); EC 1.5.3.- (fructosyl-peptide oxidase)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150408
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X15003921


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[PMID]:25344087
[Au] Autor:Chen X; Mou Y; Ling J; Wang N; Wang X; Hu J
[Ad] Endereço:Institute of Applied Ecology, Chinese Academy of Sciences, Shenyang, 110016, China.
[Ti] Título:Cyclic dipeptides produced by fungus Eupenicillium brefeldianum HMP-F96 induced extracellular alkalinization and H2O 2 production in tobacco cell suspensions.
[So] Source:World J Microbiol Biotechnol;31(1):247-53, 2015 Jan.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Extracellular alkalinization and H2O2 production are important early events during induced systemic resistance (ISR) establishment in plants. In a screen for metabolites as potential ISR activators from 98 fungal isolates associated with marine sponge Hymeniacidon perleve, the crude metabolites of fungus Eupenicillium brefeldianum HMP-F96 induced significant extracellular alkalinization coupled with H2O2 production in tobacco cell suspensions. A combined bioactivity and (1)H NMR-guided fractionation approach was used to disclose the chemical determinants responsible for the activities. Eight cyclic dipeptides were purified from the fermentation broth of the strain and were structurally characterized by NMR and MS experiments. This study represents the first report of the occurrence of cyclic dipeptides in E. brefeldianum and of their activities of inducing extracellular alkalinization and H2O2 production in tobacco cell suspensions.
[Mh] Termos MeSH primário: Adjuvantes Imunológicos/metabolismo
Álcalis/toxicidade
Eupenicillium/metabolismo
Peróxido de Hidrogênio/toxicidade
Peptídeos Cíclicos/metabolismo
Tabaco/imunologia
Tabaco/microbiologia
[Mh] Termos MeSH secundário: Adjuvantes Imunológicos/química
Adjuvantes Imunológicos/isolamento & purificação
Animais
Dipeptídeos/química
Dipeptídeos/isolamento & purificação
Dipeptídeos/metabolismo
Eupenicillium/isolamento & purificação
Espectroscopia de Ressonância Magnética
Espectrometria de Massas
Peptídeos Cíclicos/química
Peptídeos Cíclicos/isolamento & purificação
Poríferos/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Alkalies); 0 (Dipeptides); 0 (Peptides, Cyclic); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141026
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-014-1759-0


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[PMID]:25127475
[Au] Autor:Grawe GF; de Oliveira TR; de Andrade Narciso E; Moccelini SK; Terezo AJ; Soares MA; Castilho M
[Ad] Endereço:Departamento de Química, Grupo de Eletroquímica e Novos Materiais, Universidade Federal de Mato Grosso, 78060-900, Cuiabá, MT, Brazil.
[Ti] Título:Electrochemical biosensor for carbofuran pesticide based on esterases from Eupenicillium shearii FREI-39 endophytic fungus.
[So] Source:Biosens Bioelectron;63:407-13, 2015 Jan 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this work, a biosensor was constructed by physical adsorption of the isolated endophytic fungus Eupenicillium shearii FREI-39 esterase on halloysite, using graphite powder, multi-walled carbon nanotubes and mineral oil for the determination of carbofuran pesticide by inhibition of the esterase using square-wave voltammetry (SWV). Specific esterase activities were determined each 2 days over a period of 15 days of growth in four different inoculation media. The highest specific activity was found on 6th day, with 33.08 U on PDA broth. The best performance of the proposed biosensor was obtained using 0.5 U esterase activity. The carbofuran concentration response was linear in the range from 5.0 to 100.0 µg L(-1) (r=0.9986) with detection and quantification limits of 1.69 µg L(-1) and 5.13 µg L(-1), respectively. A recovery study of carbofuran in spiked water samples showed values ranging from 103.8±6.7% to 106.7±9.7%. The biosensor showed good repeatability and reproducibility and remained stable for a period of 20 weeks. The determination of carbofuran in spiked water samples using the proposed biosensor was satisfactory when compared to the chromatographic reference method. The results showed no significant difference at the 95% confidence level with t-test statistics. The application of enzymes from endophytic fungi in constructing biosensors broadens the biotechnological importance of these microorganisms.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Carbofurano/isolamento & purificação
Esterases/química
Praguicidas/isolamento & purificação
[Mh] Termos MeSH secundário: Carbofurano/química
Enzimas Imobilizadas/química
Eupenicillium/química
Eupenicillium/enzimologia
Nanotubos de Carbono/química
Praguicidas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Nanotubes, Carbon); 0 (Pesticides); EC 3.1.- (Esterases); SKF77S6Y67 (Carbofuran)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:140901
[Lr] Data última revisão:
140901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140816
[St] Status:MEDLINE


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[PMID]:25639038
[Au] Autor:Varbanets' LD; Matseliukh OV; Nidialkova NA; Hudzenko OV; Avdiiuk KV; Shmatkova NV; Seifullina II
[Ti] Título:[Influence of coordination compounds of germanium (IV) and stannum (IV) on activity of some microbial enzymes with glycolytic and proteolytic action].
[So] Source:Mikrobiol Z;76(6):11-8, 2014 Nov-Dec.
[Is] ISSN:1028-0987
[Cp] País de publicação:Ukraine
[La] Idioma:ukr
[Ab] Resumo:Influence of coordinative compounds of germanium (IV) and stanum (IV) (complexes of germanium (IV) with nicotinamide (Nad) [GeCl2(Nad)4]Cl2 (1) and complexes of stanum (IV) with 2-hydroxybenzoilhydrazone 4-dimetylaminobenzaldehide (2-OH-HBdb) [SnCl4(2-OH-Bdb-H)] (2), 3-hydroxy-2-naphtoilhydrazone 2-hydroxynaphtaldehide (3-OH-H2Lnf) [SnCl3(3-OH-HLnf)] (3) and izonicotinoilhydrazone 2-hydroxyibenzaldehide [SnCl3 (Is·H)] (4) on activity of peptidases 1 and 2 Bacillus thuringiensis, α-L-rhamnosidase Cryptococcus albidus, Eupenicillium erubescens and α-amylase Aspergillus flavus var. oryzae. Results testify that all studied compounds differ on their influence on activity of the enzymes tested: significantly don't change elastolytic activity of peptidases 1 and 2 B. thuringiensis, completely inhibit A. flavus var. oryzae amylase, activate or oppress of α-L-rhamnosidase C. albidus and E. erubescens. Considerable differences in compounds (3, 4) on activity observed in case of the last. It's possible that peculiarity of influence (1) in compare with (2-4) is connected with existence of different central atoms of complexants: germanium (IV) (1) and stanum (IV) (2-4). A certain analogy in oppression of C. albidus α-L-rhamnosidase by compounds (1) and (4) can explain with presence of a pyridinic ring at molecules of their ligands. The less activsty displayed compound (2) with coordinative knot {SnCl4ON}. Nature of compounds (3, 4) activity was absolutely different: essential increase of activity of C. albidus α-L-rhamnosidase and full oppression of E. erubescens α-L-rhamnosidase by compound (3), while the action of compound (4) was feed back. Taking into account identical coordination knot {SnCl3O2N} the major role in this case play change of a hydrazide fragment in molecules of their ligands.
[Mh] Termos MeSH primário: Anti-Infecciosos/farmacologia
Proteínas de Bactérias/metabolismo
Complexos de Coordenação/farmacologia
Proteínas Fúngicas/metabolismo
Germânio/química
Compostos Orgânicos de Estanho/farmacologia
Estanho/química
[Mh] Termos MeSH secundário: Anti-Infecciosos/síntese química
Aspergillus flavus/efeitos dos fármacos
Aspergillus flavus/enzimologia
Aspergillus flavus/crescimento & desenvolvimento
Bacillus thuringiensis/efeitos dos fármacos
Bacillus thuringiensis/enzimologia
Bacillus thuringiensis/crescimento & desenvolvimento
Proteínas de Bactérias/antagonistas & inibidores
Benzaldeídos/química
Complexos de Coordenação/síntese química
Cryptococcus/efeitos dos fármacos
Cryptococcus/enzimologia
Cryptococcus/crescimento & desenvolvimento
Eupenicillium/efeitos dos fármacos
Eupenicillium/enzimologia
Eupenicillium/crescimento & desenvolvimento
Proteínas Fúngicas/antagonistas & inibidores
Glicosídeo Hidrolases/antagonistas & inibidores
Glicosídeo Hidrolases/metabolismo
Hidrazonas/química
Testes de Sensibilidade Microbiana
NAD/química
Compostos Orgânicos de Estanho/síntese química
Peptídeo Hidrolases/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Bacterial Proteins); 0 (Benzaldehydes); 0 (Coordination Complexes); 0 (Fungal Proteins); 0 (Hydrazones); 0 (Organotin Compounds); 00072J7XWS (Germanium); 0U46U6E8UK (NAD); 7440-31-5 (Tin); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.40 (alpha-L-rhamnosidase); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:150202
[Lr] Data última revisão:
150202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150203
[St] Status:MEDLINE


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[PMID]:25434209
[Au] Autor:Hudzenko OV; Varbanets' LD
[Ti] Título:[Component composition of Cryptococcus albidus and Eupenicillium erubescens alpha-L-rhamnosidases].
[So] Source:Mikrobiol Z;76(5):8-14, 2014 Sep-Oct.
[Is] ISSN:1028-0987
[Cp] País de publicação:Ukraine
[La] Idioma:ukr
[Ab] Resumo:The component composition of Cryptococcus albidus and Eupenicillium erubescers alpha-L-rhamnosidases have studied. It was shown that enzymes have a monomeric structure. Enzyme preparations of C. albidus and E. erubescens have similar qualitative but differ in quantitative amino acid composition. alpha-L-rhamnosidase of C. albidus characterised by high amount of histidine, proline, cysteine, methionine in compared with alpha-L-rhamnosidase of E. erubescens. alpha-L-Rhamnosidase of E. erubescens, in contrast to the alpha-L-rhamnnosidase of C. albidus, contained higher levels of lysine, arginine, threonine, alanine, isoleucine, leucine, tyrosine, phenylalanine. It is shown that purified preparations of alpha-L-rhamnosidase C. albidus and E. erubescens contained 5 and 1% carbohydrates respectively. Enzyme preparations differ in quantitative monosaccharide composition, which represented by rhanmose, xylose, mannose, galactose and glucose. Furthermore, alpha-L-rhannosidase C. albidus contained fuicose, whereas alpha-L-rhamnosidase E. erubescens--ribose and arabinose. A significant percentage of hydrophobic amino acids, which is 31 and 34% of the total content, and the presence of the carbohydrate component are essential in stabilization of enzymes molecule.
[Mh] Termos MeSH primário: Cryptococcus/enzimologia
Eupenicillium/enzimologia
Glicosídeo Hidrolases/química
[Mh] Termos MeSH secundário: Aminoácidos/química
Eletroforese em Gel de Poliacrilamida
Glicosídeo Hidrolases/isolamento & purificação
Peso Molecular
Monossacarídeos/química
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Monosaccharides); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.40 (alpha-L-rhamnosidase)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:141201
[Lr] Data última revisão:
141201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141202
[St] Status:MEDLINE



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