1 Oligopeptidase
Mostrando 1-12 de 20 artigos, teses e dissertações.
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1. Estudo cinético da oligopeptidase A (OpdA) de Escherichia coli e determinação da importância do resíduo Tyr607 para sua atividade catalítica. / Kinetic study of oligopeptidase A (OPDA) from Escherichia coli and determination of the importance of residue Tyr607 to its catalytic activity.
Oligopeptidase A (OpdA) é uma peptidase bacteriana membro da subfamília M3A que apresenta propriedades catalíticas e estruturais semelhantes às das peptidases de mamífero thimet-oligopeptidase (TOP) e neurolisina (NEL). As três enzimas apresentam quatro resíduos de tirosina conservados presentes na alça flexível que se encontra próxima ao centro at
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 31/03/2010
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2. Identificação de atividade metalo-oligopeptidásica Thimet-like em Paracoccidioides brasiliensis: um novo fator de patogenicidade fúngica? / Identification of a metalo-oligopeptidasic TOP-like activity in Paracoccidioides brasiliensis: a novel factor of fungal patogenicity?
Paracoccidioides brasiliensis (Pb), é uma micose sistêmica grave com formas aguda e crônica. As proteases ou peptidases são enzimas proteolíticas que ocorrem em todos os organismos e correspondem a 1-5% de seus conteúdos genéticos. Estas enzimas estão envolvidas em processos biológicos essenciais, como a coagulação sanguínea, morte celular e dife
Publicado em: 2010
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3. Peptídeos intracelulares como novos moduladores da transdução de sinal de receptores acoplados à proteína G
A degradacao de proteinas pelo sistema ubiquitina-proteassoma gera uma grande quantidade de oligopeptideos dentro das celulas. Para investigar possiveis efeitos desses oligopeptideos, alguns deles foram isolados do cerebro de rato, sintetizados acoplados a sequencia peptidica TAT atraves de pontes dissulfeto, sendo entao analisados nas vias de transducao de
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 28/05/2008
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4. Propriedades termodinâmicas da Prolil Oligopeptidase de Trypanosoma brucei
Trypanosoma brucei secrets a prolyl oligopeptidase (POPTb) which is possibly involved in the pathogenesis of sleeping sickness. It is able to hydrolyze prolinecontaining peptide hormones and is therefore considered a good target for the development of drugs to treat the disease. As the crystal structure of POPTb has not been solved yet, we used circular dich
Publicado em: 2008
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5. NUDEL-OLIGOPEPTIDASE: ANÁLISE DA DISTRIBUIÇÃO DO RNAm NO SNC DE RATOS NEONATOS E ADULTOS E CARACTERIZAÇÃO DO RESÍDUO CRÍTICO PARA A ATIVIDADE CATALÍTICA. / NUDEL-oligopeptidase: analysis of mRNA distribution in the central nervous system (CNS) of newborn and adult rats, and characterization of the amino acid residue critical for the catalytic activity.
Thirty years ago the first endooligopeptidases were described, and named Endo A (EOPA) and Endo B. EOPA was later characterized as a thiol-activated peptidase showing specificity for substrates comprising 7 to 13 amino acid residues. In 2000, studying the molecular mechanisms of the brain disorder lissencephaly, three independent groups isolated a protein na
Publicado em: 2006
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6. Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase activity by disrupted-in-schizophrenia 1
Recently, nuclear distribution element-like (NUDEL) has been implicated to play a role in lissencephaly and schizophrenia through interactions with the lissencephaly gene 1 (Lis1) and disrupted-in-schizophrenia 1 (DISC1) products, respectively. Interestingly, NUDEL is the same protein as endooligopeptidase A (EOPA), a thiol-activated peptidase involved in co
National Academy of Sciences.
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7. Characterization of an intracellular oligopeptidase from Lactobacillus paracasei.
An intracellular oligopeptidase from Lactobacillus paracasei Lc-01 has been purified to homogeneity by Fast Flow Q Sepharose, hydroxyapatite, and Mono Q chromatography. The molecular mass of the enzyme was determined to be 140 kDa by gel filtration and approximately 30 kDa by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and SDS-capillary e
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8. Degradation of a signal peptide by protease IV and oligopeptidase A.
The degradation of the prolipoprotein signal peptide in vitro by membranes, cytoplasmic fraction, and two purified major signal peptide peptidases from Escherichia coli was followed by reverse-phase liquid chromatography (RPLC). The cytoplasmic fraction hydrolyzed the signal peptide completely into amino acids. In contrast, many peptide fragments accumulated
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9. Substrate Recognition Properties of Oligopeptidase B from Salmonella enterica Serovar Typhimurium
Oligopeptidase B (OpdB) is a serine peptidase broadly distributed among unicellular eukaryotes, gram-negative bacteria, and spirochetes which has emerged as an important virulence factor and potential therapeutic target in infectious diseases. We report here the cloning and expression of the opdB homologue from Salmonella enterica serovar Typhimurium and dem
American Society for Microbiology.
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10. Cloning and Expression of an Oligopeptidase, PepO, with Novel Specificity from Lactobacillus rhamnosus HN001 (DR20)
Oligopeptidases of starter and nonstarter lactic acid bacteria contribute to the proteolytic events important in maturation and flavor development processes in cheese. This paper describes the molecular cloning, expression, and specificity of the oligopeptidase PepO from the probiotic nonstarter strain Lactobacillus rhamnosus HN001 (DR20). The pepO gene enco
American Society for Microbiology.
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11. An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides.
An endo-acting proline-specific oligopeptidase (prolyl oligopeptidase [POPase], EC 3.4.21.26) was purified to homogeneity from the Triton X-100 extracts of cells of Treponema denticola ATCC 35405 (a human oral spirochete) by a procedure that comprised five successive fast protein liquid chromatography steps. The POPase is a cell-associated 75- to 77-kDa prot
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12. Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity
Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30 amino acids. POP may be associated with cognitive functions, possibly via the cleavage of neuropeptides. Recent studies have also suggested novel non-hydrolytic and non-catalytic functions for POP. Moreover, POP has also been proposed as a regula
Histochemical Society.