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Glycosidase- and ß-lactamase-like activity of dinuclear copper(II) patellamide complexes.
Comba, Peter; Eisenschmidt, Annika; Kipper, Nora; Schießl, Jasmin.
Afiliação
  • Comba P; University of Heidelberg, Institute of Inorganic Chemistry and Interdisciplinary Center for Scientific Computing, Im Neuenheimer Feld 270, D-69120 Heidelberg, Germany.
  • Eisenschmidt A; University of Heidelberg, Institute of Inorganic Chemistry and Interdisciplinary Center for Scientific Computing, Im Neuenheimer Feld 270, D-69120 Heidelberg, Germany.
  • Kipper N; University of Heidelberg, Institute of Inorganic Chemistry and Interdisciplinary Center for Scientific Computing, Im Neuenheimer Feld 270, D-69120 Heidelberg, Germany.
  • Schießl J; University of Heidelberg, Institute of Inorganic Chemistry and Interdisciplinary Center for Scientific Computing, Im Neuenheimer Feld 270, D-69120 Heidelberg, Germany.
J Inorg Biochem ; 159: 70-5, 2016 06.
Article em En | MEDLINE | ID: mdl-26921720
Prochloron, a blue-green algae belonging to ancient prokaryotes, produces, like other cyanobacteria, cyclic pseudo-peptides, which are also found in its obligate symbiont ascidiae (Lissoclinum patellum). Although research has focused for some time on the putative metabolic function of these cyclic peptides, to date it is still not understood. Their role might be connected to the increased concentrations of divalent metal ions, especially Cu(II), found in ascidiae. Dinuclear copper(II) complexes of cyclic pseudo-peptides revealed a broad hydrolytic capacity, including carboanhydrase and phosphatase activity. This study reports their ß-lactamase as well as α- and ß-glycosidase activity with kcat=(11.34±0.91)ˑ10(-4)s(-1) for ß-lactamase, kcat=(1.55±0.13)ˑ10(-4)s(-1) for α-glycosidase and kcat=(1.22±0.09)ˑ10(-4)s(-1) for ß-glycosidase activity.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos Cíclicos / Proteínas de Bactérias / Beta-Lactamases / Cianobactérias / Cobre / Glicosídeo Hidrolases Limite: Animals Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos Cíclicos / Proteínas de Bactérias / Beta-Lactamases / Cianobactérias / Cobre / Glicosídeo Hidrolases Limite: Animals Idioma: En Ano de publicação: 2016 Tipo de documento: Article