Serine Endopeptidases
Mostrando 1-12 de 17 artigos, teses e dissertações.
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1. Identificação e caracterização de inibidores de serino-endopeptidases (serpinas) em Rhipicephalus (Boophilus) microplus
Carrapatos são animais hematófagos transmissores de diversas doenças para animais e seres humanos. O Rhipicephalus (Boophilus) microplus é um ectoparasito específico de bovinos. É responsável por importantes perdas econômicas na pecuária de países produtores de carne e leite. O aumento de populações de carrapatos resistentes aos principais acaric
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 2012
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2. Purification, kinetics and physical-chemistry characterization of periplaneta americana, Tenebrio molitor and Diatraca saccharalis digestive chymotrypsin / Purificação, caracterização físico-químico e cinética das quimotripsinas digestivas de Periplaneta americana, Tenebrio molitor e Diatraea saccharalis.
Chymotrypsins (EC 3.4.21.1) are serine proteases with 245 amino acids disposed in two double ?-barrel domains, being the active site locate between these two domains. The specificity study of endopeptidases was facilitated by the substrate binding site concept that is the active site of these enzymes. However there is not much information about the subsites
Publicado em: 2006
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3. Insect serine-endopeptidases and plant-insect interactions / Serina endopeptidases de insetos e a interação inseto-planta
Serina endopeptidases de insetos, principalmente tripsinas e quimotripsinas, estão envolvidas na digestão inicial de proteínas. Genes codificadores para estas enzimas estão organizados em famílias multigênicas tendo expressão diferencial de acordo com a dieta do inseto, estando envolvidos no desenvolvimento de resistência a diferentes metabólitos se
Publicado em: 2004
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4. Site-Specific Serine Incorporation by Lif and Epr into Positions 3 and 5 of the Staphylococcal Peptidoglycan Interpeptide Bridge
The FemAB-like factors Lif and Epr confer resistance to glycylglycine endopeptidases lysostaphin and Ale-1, respectively, by incorporating serine residues into the staphylococcal peptidoglycan interpeptide bridges specifically at positions 3 and 5. This required the presence of FemA and/or FemB, in contrast to earlier postulations.
American Society for Microbiology.
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5. Homologous inhibitors from potato tubers of serine endopeptidases and metallocarboxypeptidases.
A potent polypeptide inhibitor of chymotrypsin has been purified from Russett Burbank potatoes. The inhibitor has no effect on bovine carboxypeptidases A or B but exhibits homology with a carboxypeptidase inhibitor that is also present in potato tubers. The chymotrypsin inhibitor has a molecular weight of approximately 5400 as estimated by gel filtration, am
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6. Identification of active-site residues of the adenovirus endopeptidase.
Multiple sequence alignment of the 12 adenovirus endopeptidases known to date identified a number of conserved residues which might be important for enzyme activity. Eleven mutants were created in the cloned gene by site-directed mutagenesis to identify the active site of this thiol endopeptidase. Analysis of the proteolytic activity in a crude system using
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7. Peptidohydrolases of Soybean Root Nodules 12: IDENTIFICATION, SEPARATION, AND PARTIAL CHARACTERIZATION OF ENZYMES FROM BACTEROID-FREE EXTRACTS
Nodule extracts prepared from Glycine max var Woodworth possessed endopeptidase, aminopeptidase, and carboxypeptidase activities. Three distinct endopeptidase activities could be resolved by disc-gel electrophoresis at pH 8.8. According to their order of increasing electrophoretic mobility, the first of these enzymes hydrolyzed azocasein and n-benzoyl-l-Leu-
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8. Purification and Characterization of a Substrate-Size-Recognizing Metalloendopeptidase from Streptococcus cremoris H61
During the ripening of Gouda-type cheese, two kinds of endopeptidases were found to participate in the degradation of αs1-CN(f1-23), a specific product from αs1-casein hydrolyzed by chymosin. One of the endopeptidases, lactic acid bacteria endopeptidase (LEP-II), which can recognize the size of its substrates, has already been purified and characterized (T
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9. Proline-specific endopeptidases from microbial sources: isolation of an enzyme from a Xanthomonas sp.
An extensive screening among microorganisms for the presence of post-proline-specific endopeptidase activity was performed. This activity was found among ordinary bacteria from soil samples but not among fungi and actinomycetes. This result is in contrast to the previous notion that this activity is confined to the genus Flavobacterium. A proline endopeptida
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10. Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity
Prolyl endopeptidases (PEPs) are a unique class of serine proteases with considerable therapeutic potential for the treatment of celiac sprue. The crystal structures of two didomain PEPs have been solved in alternative configurations, thereby providing insights into the mode of action of these enzymes. The structure of the Sphingomonas capsulata PEP, solved
National Academy of Sciences.
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11. Characterization of a maize root proteinase.
The major proteinase in maize (Zea mays) roots behaves as a serine endopeptidase. A possible physiological role of this enzyme could be in the turnover of nitrate reductase (NR) and, as such, it could be of great importance in regulating the assimilation of nitrate. The objective of this research was to elucidate the specificity and uniqueness of maize root
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12. Self Purification of Two Serine Endopeptidases*
We have reported that a serine protease from Pronase, homologous with bovine chymotrypsin, is both active and stable in 6 M guanidinium chloride. The present investigation examined the possibility that this unique property might be used to permit the enzyme to engage in its own purification by cleaving companion proteins to low-molecular-weight products. Ana