TY - JOUR
T1 - Non-native states of cardosin a induced by acetonitrile
T2 - activity modulation via polypeptide chains rearrangements
AU - Oliveira, Cláudia S.
AU - Sarmento, A. Cristina
AU - Pereira, Anabela
AU - Correia, Isabel
AU - Pessoa, João Costa
AU - Esteves, Valdemar I.
AU - Fonseca, Henrique M.A.C.
AU - Pires, Euclides
AU - Barros, Marlene T.
PY - 2009/12
Y1 - 2009/12
N2 - 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.
AB - 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.
KW - Acetonitrile
KW - Aspartic proteinases
KW - Cardosin A
KW - Folding
UR - http://www.scopus.com/inward/record.url?scp=72149096808&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2009.08.003
DO - 10.1016/j.molcatb.2009.08.003
M3 - Article
AN - SCOPUS:72149096808
SN - 1381-1177
VL - 61
SP - 274
EP - 278
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
IS - 3-4
ER -
