Non-native states of cardosin a induced by acetonitrile: activity modulation via polypeptide chains rearrangements

Cláudia S. Oliveira*, A. Cristina Sarmento, Anabela Pereira, Isabel Correia, João Costa Pessoa, Valdemar I. Esteves, Henrique M.A.C. Fonseca, Euclides Pires, Marlene T. Barros

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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 a member of 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 the enzyme activity 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.

Original languageEnglish
Pages (from-to)274-278
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Volume61
Issue number3-4
DOIs
Publication statusPublished - Dec 2009

Keywords

  • Acetonitrile
  • Aspartic proteinases
  • Cardosin A
  • Folding

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