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An X‐ray solution scattering study of the cofactor and activator induced structural changes in yeast pyruvate decarboxylase (PDC)
Author(s) -
Hübner G.,
König S.,
Schellenberger A.,
Koch M.H.J.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81495-a
Subject(s) - pyruvate decarboxylase , tetramer , cofactor , chemistry , yeast , dissociation (chemistry) , enzyme , kinetics , activator (genetics) , biochemistry , crystallography , biophysics , stereochemistry , biology , physics , quantum mechanics , gene , alcohol dehydrogenase
Structure and activation pattern of pyruvate decarboxylase (PDC) from yeast was studied by synchrotron radiation X‐ray solution scattering. The results give a direct proof that the reversible deactivation of PDC at pH 8.0 is accompanied by the dissociation of the tetrameric holoenzyme into dimeric halves. The kinetics of this process was followed. At pH 6.5 the dimeric halves reassociate to a tetramer even in the absence of cofactors. The changes of the scattering pattern upon binding of the substrate‐like activator pyruvamide indicate that the structure expands in the course of the enzyme activation.