TAILIEUCHUNG - Báo cáo khoa học: Biochemical characterization and structural prediction of a novel cytosolic leucyl aminopeptidase of the M17 family from Schizosaccharomyces pombe

A new leucyl aminopeptidase activity has been identified in the fission yeast Schizosaccharomyces pombe. The enzyme, which has been purified and named leucyl aminopeptidase yspII (LAP yspII), had a molecular mass of 320 and 54 kDa by gel filtration and SDS⁄PAGE, respectively, suggesting a homohexameric structure. | ễFEBS Journal Biochemical characterization and structural prediction of a novel cytosolic leucyl aminopeptidase of the M17 family from Schizosaccharomycespombe Irma Herrera-Camacho1 Nora H. Rosas-Murrieta1 Arturo Rojo-Dominguez2 Lourdes Millan1 Julio Reyes-Leyva3 Gerardo Santos-Lopez3 and Paz Suarez-Rendueles4 1 Laboratorio de Bioquimica y Biologia Molecular Centro de Quimica del Institute de Ciencias Universidad Autonoma de Puebla Puebla Mexico 2 Departamentos de Ciencias Naturales-Cuajimalpa y de Quimica-Iztapalapa Universidad Autonoma Metropolitana Mexico D. F. Mexico 3 Laboratorio de Virologia y Biologia Molecular Centro de Investigacion Biomedica de Oriente IMSS Atlixco-Metepec Puebla Mexico 4 Departamento de Bioquimica y Biologia Molecular. Facultad de Medicina Universidad de Oviedo Spain Keywords catalytic mechanism LAP yspll leucyl aminopeptidase M17 family of peptidases model structure Correspondence I. Herrera-Camacho Laboratorio de Bioquimica y Biologia Molecular. Centro de Quimica del Instituto de Ciencias Universidad Autonoma de Puebla Apartado postal 1613 72000 Puebla Pue Mexico Fax 52 222 2295551 Tel 52 222 2295500 E-mail pherrera@ Received 21 June 2007 revised 10 October 2007 accepted 15 October 2007 doi A new leucyl aminopeptidase activity has been identified in the fission yeast Schizosaccharomyces pombe. The enzyme which has been purified and named leucyl aminopeptidase yspII LAP yspII had a molecular mass of 320 and 54 kDa by gel filtration and SDS PAGE. respectively suggesting a homohexameric structure. The enzyme cleaved synthetic aminoacyl-4-nitroanilides at an optimum of pH and preferred leucine and methionine as N-terminal amino acids. A clear dependence on Mn2 concentration for activity was found and an apparent association constant of mM was calculated for the metal ion. Bestatin behaved as a competitive inhibitor of LAP yspII Ki pM while chelating agents such as .

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