Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add filters








Year range
1.
Mem. Inst. Oswaldo Cruz ; 104(3): 505-512, May 2009. ilus
Article in English | LILACS | ID: lil-517023

ABSTRACT

Aspartyl proteases are a class of enzymes that include the yeast aspartyl proteases and secreted aspartyl protease (Sap) superfamilies. Several Sap superfamily members have been demonstrated or suggested as virulence factors in opportunistic pathogens of the genus Candida. Candida albicans, Candida tropicalis, Candida dubliniensis and Candida parapsilosis harbour 10, four, eight and three SAP genes, respectively. In this work, genome mining and phylogenetic analyses revealed the presence of new members of the Sap superfamily in C. tropicalis (8), Candida guilliermondii (8), C. parapsilosis(11) and Candida lusitaniae (3). A total of 12 Sap families, containing proteins with at least 50 percent similarity, were discovered in opportunistic, pathogenic Candida spp. In several Sap families, at least two subfamilies or orthologous groups were identified, each defined by > 90 percent sequence similitude, functional similarity and synteny among its members. No new members of previously described Sap families were found in a Candida spp. clinical strain collection; however, the universality of SAPT gene distribution among C. tropicalis strains was demonstrated. In addition, several features of opportunistic pathogenic Candida species, such as gene duplications and inversions, similitude, synteny, putative transcription factor binding sites and genome traits of SAP gene superfamily were described in a molecular evolutionary context.


Subject(s)
Aspartic Acid Endopeptidases/genetics , Candida/enzymology , Evolution, Molecular , Phylogeny , Candida/classification , Candida/genetics , DNA, Fungal/genetics , Genes, Fungal
2.
Rev. latinoam. microbiol ; 31(1): 71-6, ene.-mar. 1989. ilus, tab
Article in Spanish | LILACS | ID: lil-94141

ABSTRACT

Se hizo un estudio comparativo en cuanto a la producción de enzimas por ima ceá de Streptomyces sp, utilizando como substrato caparazón de camarón desmineralizado ó quitina semipurificada. Se encontró que la producción de quitinasas está asociada al crecimiento microbiano cuando se usa como substrato caparazón de camarón, alcanzando una producción máxima de quitinasa, qutitosanasa, carboximetilcelulasa y de proteasa a las 96 h de incubación. Cuando el substrato fue la quitina, se obtuvo un máximo en la producción quitinolítica y quitosanolítica al alcanzar la fase de crecimiento estacionario. El crecimiento de Streptomyces sp fue mayor en caparazón de camarón que en quitina, siendo muy pequeñas las velocidades específicas de crecimiento tanto en caparazón de camarón como en quitina semipurificada


Subject(s)
Animals , Enzymes/isolation & purification , In Vitro Techniques , Streptomyces/drug effects , Carboxymethylcellulose Sodium/analogs & derivatives , Chitin/isolation & purification
SELECTION OF CITATIONS
SEARCH DETAIL