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 Non-native states of cardosin A induced by acetonitrile: Activity modulation via polypeptide chains rearrangements
Please use this identifier to cite or link to this item http://hdl.handle.net/10773/6781

title: Non-native states of cardosin A induced by acetonitrile: Activity modulation via polypeptide chains rearrangements
authors: Oliveira, Claudia S.
Sarmento, A. Cristina
Pereira, Anabela
Correia, Isabel
Pessoa, Joao Costa
Esteves, Valdemar I.
Fonseca, Henrique M. A. C.
Pires, Euclides
Barros, Marlene T.
keywords: Cardosin A
Aspartic proteinases
issue date: 2009
publisher: Elsevier
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.
URI: http://hdl.handle.net/10773/6781
ISSN: 1381-1177
publisher version/DOI: http://dx.doi.org/10.1016/j.molcatb.2009.08.003
source: Journal of Molecular Catalysis B: Enzymatic
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