Base de dados : MEDLINE
Pesquisa : D04.345.566.515 [Categoria DeCS]
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  1 / 28 MEDLINE  
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[PMID]:9579085
[Au] Autor:Chowdhury B; Das SK; Bose SK
[Ad] Endereço:Department of Biochemistry, University College of Science, Calcutta, India.
[Ti] Título:Use of resistant mutants to characterize the target of mycobacillin in Aspergillus niger membranes.
[So] Source:Microbiology;144 ( Pt 4):1123-30, 1998 Apr.
[Is] ISSN:1350-0872
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mycobacillin-sensitive Aspergillus niger strain G3Br and resistant mutants of it did not show any differences in their total lipid content, although the amounts of phospholipids and sterols, particularly phosphatidylcholine and cholesterol, were lower in resistant cells. Mycobacillin resistance was accompanied by an increase in the phase-transition temperature of plasma membrane preparations. When exposed to mycobacillin, resistant and sensitive cells did not differ qualitatively with respect to most released materials (lysine, proline, Pi, Na+, K+, Ca2+); however, the release of ATP was completely inhibited in resistant cells unless they were exposed to concentrations of mycobacillin exceeding their respective MIC value. Resistant cells, under steady-state conditions, displayed greater uptake and release of the same specific materials--except ATP--as sensitive cells did under similar conditions. Thus release and uptake of those materials except ATP are not implicated in the mode of action of mycobacillin. The inhibiting action of mycobacillin (at concentrations higher than the MIC) on sensitive or resistant cells was completely antagonized by ATP (which did not form any complex with mycobacillin) but not by any of the releasable components, either alone or in combination. This observation, coupled with the authors' recent findings on ATP release, indicates that the fungistatic action of mycobacillin is due to excessive ATP release, leading to energy starvation. Interestingly, ATP release during the first 2 h of incubation with mycobacillin was minimal, but increased to over 96% during the next 48 h. Release and uptake of ATP via liposomes, prepared with lipid and protein isolated from membranes of the mycobacillin-sensitive parent and resistant mutants, showed that mycobacillin action could be inhibited either by resistant protein or by resistant lipid. The mycobacillin target appears to be a lipid-protein site on the membrane of sensitive A. niger G3Br.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Aspergillus niger/efeitos dos fármacos
Micobacilina/farmacologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Aspergillus niger/química
Aspergillus niger/crescimento & desenvolvimento
Proteínas de Transporte/metabolismo
Permeabilidade da Membrana Celular/efeitos dos fármacos
Lipídeos de Membrana/metabolismo
Testes de Sensibilidade Microbiana
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Carrier Proteins); 0 (Membrane Lipids); 18524-67-9 (Mycobacillin); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:9806
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:980514
[St] Status:MEDLINE


  2 / 28 MEDLINE  
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[PMID]:1655689
[Au] Autor:Bhaduri S; Bose SK
[Ad] Endereço:Department of Biochemistry, University College of Science, Calcutta, India.
[Ti] Título:Catabolite repression vs derepression, an approach to differentiation during sporulation in Bacillus subtilis.
[So] Source:J Appl Bacteriol;71(2):147-53, 1991 Aug.
[Is] ISSN:0021-8847
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glutamine, like glucose, repressed sporulation and the synthesis of mycobacillin and dipicolinic acid by Bacillus subtilis, and these syntheses were depressed by dibutyryl cyclic GMP but not by dibutyryl cyclic AMP. Neither of these dibutyryl cyclic nucleotides affected sporulation or a number of spore-associated parameters in the strain under normal physiological conditions. Mutants insensitive to glutamine repression were indifferent to the addition of either of the dibutyryl cyclic nucleotides both in the presence and in the absence of glutamine. Sporulation resulted from the remission of repression obtained under the catabolically active state.
[Mh] Termos MeSH primário: Bacillus subtilis/fisiologia
[Mh] Termos MeSH secundário: Bacillus subtilis/efeitos dos fármacos
Bacillus subtilis/genética
Bucladesina/farmacologia
Dibutiril GMP Cíclico/farmacologia
Glutamina/farmacologia
Mutação
Micobacilina/biossíntese
Ácidos Picolínicos/metabolismo
Esporos Bacterianos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Picolinic Acids); 0RH81L854J (Glutamine); 18524-67-9 (Mycobacillin); 32266-35-6 (Dibutyryl Cyclic GMP); 63X7MBT2LQ (Bucladesine); UE81S5CQ0G (dipicolinic acid)
[Em] Mês de entrada:9111
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:910801
[St] Status:MEDLINE


  3 / 28 MEDLINE  
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[PMID]:3143803
[Au] Autor:Majumder S; Mukhopadhyay NK; Ghosh SK; Bose SK
[Ad] Endereço:Department of Biochemistry, University College of Science, Calcutta, India.
[Ti] Título:Genetic analysis fo the mycobacillin biosynthetic pathway in Bacillus subtilis B3.
[So] Source:J Gen Microbiol;134(5):1147-53, 1988 May.
[Is] ISSN:0022-1287
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Twelve mycobacillin-negative (My-) mutants of Bacillus subtilis B3 were isolated from an auxotrophically tagged mycobacillin producer organism. In whole-cell fermentations of some of these My- mutants a penta- and a nonapeptide accumulated; these peptides were also obtained in a cell-free system in which a new tripeptide was also detected. The amino acid composition, N- and C-terminal residues and amino acid sequence of these peptides agreed with those of equivalent segments of the mycobacillin molecule. The mycobacillin-synthesizing enzyme can be divided into three fractions that catalyse different steps in biosynthesis, and the defective enzyme fractions in the various mutant strains were identified by reconstitution experiments in vitro. The defects were further pin-pointed in mutant enzyme fractions by an ATP in equilibrium Pi exchange reaction and also by cell-free synthesis involving the use of membrane-bound enzyme. The defects so identified indicated the formation of tri-, penta- and nonapeptides as intermediates in the mycobacillin biosynthetic pathway.
[Mh] Termos MeSH primário: Antifúngicos/biossíntese
Bacillus subtilis/metabolismo
Micobacilina/biossíntese
[Mh] Termos MeSH secundário: Aminoácidos/metabolismo
Bacillus subtilis/enzimologia
Bacillus subtilis/genética
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Antifungal Agents); 18524-67-9 (Mycobacillin)
[Em] Mês de entrada:8901
[Cu] Atualização por classe:091119
[Lr] Data última revisão:
091119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:880501
[St] Status:MEDLINE


  4 / 28 MEDLINE  
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[PMID]:3624066
[Au] Autor:Das SK; Mukherjee S; Majumdar S; Basu S; Bose SK
[Ti] Título:Physico-chemical interaction of mycobacillin with Aspergillus niger protoplast membrane, the site of its action.
[So] Source:J Antibiot (Tokyo);40(7):1036-43, 1987 Jul.
[Is] ISSN:0021-8820
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Mycobacillin partially quenched the strong fluorescence when 1-anilino naphthalene 8-sulfonate (ANS) was added to protoplast or plasma membrane but is without any effect on weak fluorescence when added to cell-free extract. There are two classes of ANS binding sites on protoplast or plasma membrane of which one class is sensitive to mycobacillin, being competitively abolished by it. Mycobacillin also non-competitively inhibits the binding of pyrene, a lipid specific probe. Thus it follows from the inhibition by mycobacillin of ANS or pyrene binding to protoplast or plasma membrane that the site of action of the antibiotic is located in the plasma membrane. Interaction between mycobacillin and the plasma membrane is physico-chemical in nature.
[Mh] Termos MeSH primário: Antifúngicos/metabolismo
Aspergillus niger/ultraestrutura
Micobacilina/metabolismo
[Mh] Termos MeSH secundário: Naftalenossulfonato de Anilina
Aspergillus niger/metabolismo
Sítios de Ligação
Fenômenos Químicos
Química Física
Matemática
Membranas/metabolismo
Pirenos/metabolismo
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anilino Naphthalenesulfonates); 0 (Antifungal Agents); 0 (Pyrenes); 18524-67-9 (Mycobacillin); 630I4V6051 (1-anilino-8-naphthalenesulfonate); 9E0T7WFW93 (pyrene)
[Em] Mês de entrada:8710
[Cu] Atualização por classe:161123
[Lr] Data última revisão:
161123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:870701
[St] Status:MEDLINE


  5 / 28 MEDLINE  
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[PMID]:3753434
[Au] Autor:Mukhopadhyay NK; Majumder S; Ghosh SK; Bose SK
[Ti] Título:Characterization of three-fraction mycobacillin synthetase.
[So] Source:Biochem J;235(3):639-43, 1986 May 01.
[Is] ISSN:0264-6021
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mycobacillin synthetase lacks aspartic acid racemase, alanine racemase and glutamic acid racemase activities. The enzyme also does not respond to ATP-[32P]Pi exchange, nor does it catalyse the antibiotic synthesis in presence of amino acids of configuration opposite to that present in the molecule. Preincubation with optical isomers of opposite configuration inhibited the ATP-[32P]Pi exchange reaction to the extent of 60-90%. None of the three fractions of mycobacillin synthetase contained a pantothenic acid arm. Two molecules of ATP are required to synthesize one peptide bond of mycobacillin. Intermediate peptides of mycobacillin are not covalently linked to the three-fraction mycobacillin synthetase.
[Mh] Termos MeSH primário: Complexos Multienzimáticos/metabolismo
Peptídeo Sintases/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Aminoácidos/metabolismo
Micobacilina/metabolismo
Fosfatos/metabolismo
Conformação Proteica
Racemases e Epimerases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Multienzyme Complexes); 0 (Phosphates); 18524-67-9 (Mycobacillin); 8L70Q75FXE (Adenosine Triphosphate); EC 5.1.- (Racemases and Epimerases); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (mycobacillin synthetase)
[Em] Mês de entrada:8610
[Cu] Atualização por classe:170219
[Lr] Data última revisão:
170219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:860501
[St] Status:MEDLINE


  6 / 28 MEDLINE  
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[PMID]:3710916
[Au] Autor:Das SK; Majumdar S; Basu S; Mukherjee S; Bose SK
[Ti] Título:Selective action of mycobacillin on the cellular permeability of Aspergillus niger.
[So] Source:J Antibiot (Tokyo);39(4):581-8, 1986 Apr.
[Is] ISSN:0021-8820
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Cells of Aspergillus niger normally release not all but of some specific cell constituents viz., lysine, proline, ATP, Pi, Na+, K+ and Ca2+ in the absence of mycobacillin. Mycobacillin enhances the release of these materials without causing lysis. The time and concentration of mycobacillin for optimum release depends on the nature of the materials involved.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Aspergillus niger/efeitos dos fármacos
Permeabilidade da Membrana Celular/efeitos dos fármacos
Micobacilina/farmacologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Aspergillus niger/metabolismo
Relação Dose-Resposta a Droga
Eletrólitos/metabolismo
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Electrolytes); 18524-67-9 (Mycobacillin); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:8607
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:860401
[St] Status:MEDLINE


  7 / 28 MEDLINE  
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[PMID]:3103608
[Au] Autor:Ghosh SK; Majumder S; Mukhopadhyay NK; Bose SK
[Ti] Título:Role of ATP and enzyme-bound nascent peptides in the control of elongation for mycobacillin synthesis.
[So] Source:Biochem J;240(1):265-8, 1986 Nov 15.
[Is] ISSN:0264-6021
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The enzyme fraction A, a constituent of the three-fraction (A, B and C) enzyme complex mycobacillin synthetase, elongated tri- and tetra-peptides, under enzyme-bound conditions, to tetra- and penta-peptides respectively in the presence of the 'next' amino acid (in the mycobacillin sequence). The enzyme fraction B synthesized hexapeptide from free pentapeptide and the next amino acid, but synthesized heptapeptide from hexapeptide only under enzyme-bound conditions in the presence of the next amino acid. Similarly, the enzyme fraction C synthesized decapeptide from free nonapeptide in the presence of the next amino acid, but undecapeptide only from enzyme-bound decapeptide in the presence of the next amino acid during the elongation process. The Km values for the initiating reactions for each of the three enzyme fractions were 6-7-fold lower than those for the succeeding reactions catalysed by each of the enzyme fractions. The specificity of the initiation and elongation is discussed in the light of these findings.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Antifúngicos/biossíntese
Complexos Multienzimáticos/metabolismo
Micobacilina/biossíntese
Elongação Traducional da Cadeia Peptídica
Peptídeo Sintases/metabolismo
Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Bacillus subtilis/enzimologia
Bacillus subtilis/metabolismo
Cinética
Substâncias Macromoleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Macromolecular Substances); 0 (Multienzyme Complexes); 0 (Peptides); 18524-67-9 (Mycobacillin); 8L70Q75FXE (Adenosine Triphosphate); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (mycobacillin synthetase)
[Em] Mês de entrada:8703
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:861115
[St] Status:MEDLINE


  8 / 28 MEDLINE  
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[PMID]:3101663
[Au] Autor:Das SK; Basu S; Majumdar S; Bose SK
[Ti] Título:Selective action of mycobacillin on the uptake of releasable cell materials by Aspergillus niger.
[So] Source:Biochem J;239(2):317-23, 1986 Oct 15.
[Is] ISSN:0264-6021
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The uptake of normally releasable (i.e. releasable in the absence of the antibiotic) cell constituents (namely lysine, proline, ATP, Pi, Na+, K+ and Ca2+) by sensitive cells of Aspergillus niger that occurs in the absence of mycobacillin is gradually enhanced with increase in concentration of the antibiotic until the uptake attains the maximum. With still higher concentrations the uptake decreases until it becomes the same as in the control without mycobacillin. Uptake follows saturation kinetics both in the absence and in the presence of the antibiotic. Mycobacillin significantly increases Vmax. for uptake with any effect on Km, Mycobacillin has no action on the uptake of non-releasable materials.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Aspergillus niger/metabolismo
Micobacilina/farmacologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Aspergillus niger/citologia
Aspergillus niger/efeitos dos fármacos
Cálcio/metabolismo
Cinética
Lisina/metabolismo
Fosfatos/metabolismo
Potássio/metabolismo
Prolina/metabolismo
Sódio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Phosphates); 18524-67-9 (Mycobacillin); 8L70Q75FXE (Adenosine Triphosphate); 9DLQ4CIU6V (Proline); 9NEZ333N27 (Sodium); K3Z4F929H6 (Lysine); RWP5GA015D (Potassium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:8703
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:861015
[St] Status:MEDLINE


  9 / 28 MEDLINE  
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[PMID]:3093340
[Au] Autor:Majumdar S; Basu S; Das SK; Bose SK
[Ti] Título:Relationship between sporulation and synthesis of mycobacillin and dipicolinic acid under condition of catabolite repression in Bacillus subtilis.
[So] Source:Folia Microbiol (Praha);31(3):196-202, 1986.
[Is] ISSN:0015-5632
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sporulation was repressed in the parent strain by various carbon sources whereas glucose-resistant mutants were resistant to them but not to glycerol 2-phosphate. Both mycobacillin and dipicolinic acid synthesis were repressed in the parent by some of the compounds tested, viz. glucose, pyruvate and glycerol 2-phosphate. However, these syntheses in the glucose-resistant mutants were not repressed by glucose and pyruvate but were repressed by glycerol 2-phosphate. The possible interrelationship between sporulation, dipicolinic acid and mycobacillin synthesis is discussed in light of these findings.
[Mh] Termos MeSH primário: Antifúngicos/biossíntese
Bacillus subtilis/fisiologia
Micobacilina/biossíntese
Ácidos Picolínicos/biossíntese
[Mh] Termos MeSH secundário: Bacillus subtilis/metabolismo
Glucose/metabolismo
Glicerofosfatos/metabolismo
Piruvatos/metabolismo
Esporos Bacterianos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Glycerophosphates); 0 (Picolinic Acids); 0 (Pyruvates); 18524-67-9 (Mycobacillin); IY9XDZ35W2 (Glucose); UE81S5CQ0G (dipicolinic acid)
[Em] Mês de entrada:8610
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:860101
[St] Status:MEDLINE


  10 / 28 MEDLINE  
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[PMID]:4062879
[Au] Autor:Ghosh SK; Majumder S; Mukhopadhyay NK; Bose SK
[Ti] Título:Functional characterization of constituent enzyme fractions of mycobacillin synthetase.
[So] Source:Biochem J;230(3):785-9, 1985 Sep 15.
[Is] ISSN:0264-6021
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The enzyme fraction A, a constituent enzyme of the three-fraction enzyme mycobacillin synthetase, independently and sequentially activated five amino acids starting from L-proline, producing the pentapeptide Pro(Asp1,Glu1,Tyr1)Asp. The fractions B and C were unable to function independently. However, the fraction B synthesized the nonapeptide Pro(Asp3,Glu1,Tyr2,Ser1)Leu, sequentially activating the pentapeptide and next four amino acids, whereas the fraction C synthesized mycobacillin by the sequential activation of the nonapeptide and the remaining four amino acids. The pH optima of the above enzymes are almost identical (pH 7.8), but their Km values are a little different.
[Mh] Termos MeSH primário: Complexos Multienzimáticos/metabolismo
Peptídeo Sintases/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Aminoácidos/metabolismo
Concentração de Íons de Hidrogênio
Cinética
Micobacilina/biossíntese
Biossíntese Peptídica
Fosfatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Multienzyme Complexes); 0 (Phosphates); 18524-67-9 (Mycobacillin); 8L70Q75FXE (Adenosine Triphosphate); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (mycobacillin synthetase)
[Em] Mês de entrada:8512
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:850915
[St] Status:MEDLINE



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