Please use this identifier to cite or link to this item
|title: ||Non-native states of cardosin A induced by acetonitrile: Activity modulation via polypeptide chains rearrangements|
|authors: ||Oliveira, Claudia S.|
Sarmento, A. Cristina
Pessoa, Joao Costa
Esteves, Valdemar I.
Fonseca, Henrique M. A. C.
Barros, Marlene T.
|keywords: ||Cardosin A|
|issue date: ||2009|
|abstract: ||Cardosin A (EC: 3.4.23) is an enzyme containing two polypeptide chains, purified from pistils of Cynara
cardunculus L., a cardoon, used for milk clotting in cheese making. It is amemberof the aspartic proteinases
(APs), like pepsin and HIV-proteinase that are composed by two symmetric units comprising the active
site. Cardosin A is thought to be involved in many cellular events such as in pollen–pistil interaction and
adhesion dependent recognition mechanisms. In the present study, the structural and activity effects of
different amounts of acetonitrile (ACN) in cardosin A are presented. The results indicate that low ACN
concentrations (up to 10% ACN) reversibly stimulate theenzymeactivity accompanied by slight secondary
structure induction. In light of the structural and stability studies performed so far, cardosin A can adopt
conformational alterations that can result in activity modulation via polypeptide chains rearrangements.|
|publisher version/DOI: ||http://dx.doi.org/10.1016/j.molcatb.2009.08.003|
|source: ||Journal of Molecular Catalysis B: Enzymatic|
|appears in collections||DQ - Artigos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.