PMID: 9434116Jan 20, 1998Paper

Multiple unfolded states of UDP-galactose 4-epimerase from yeast Kluyveromyces fragilis. Involvement of proline cis-trans isomerization in reactivation

Biochimica Et Biophysica Acta
S DuttaDebasish Bhattacharyya

Abstract

UDP-galactose 4-epimerase from yeast Kluyveromyces fragilis is a dimeric molecule of 75 kDa per subunit with one molecule of cofactor NAD per dimer. It undergoes unfolding and complete dissociation in presence of 8 M urea at pH 7.0 by 10 min. It can be functionally reconstituted almost quantitatively in 2 h by dilution with 20 mM sodium phosphate buffer, pH 7 containing 1 mM extraneous NAD under a second order kinetics [Bhattacharyya, D. (1993) Biochemistry 32, 9726-9734]. Denaturation between 10-60 min inversely affects both the rate and maximum recovery of activity upon refolding. Aggregation of this protein has not been observed under these conditions. The time dependent reaction at the unfolded state is independent of pH between 5.4-10.4 but strongly dependent on temperature of denaturation between 0-20 degrees C. Unfolding at 0 degrees C divides the protein largely into two populations-34% of fast folding species following an apparent first order kinetics and 59% of slow folding species following a second order kinetics of reactivation. A very fast folding species of low abundance 3.5-7.5% depending on temperature of denaturation has been identified, which gets active status within the dead time of mixing. Interaction with...Continue Reading

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Citations

Aug 21, 2003·Analytical Biochemistry·Sangeeta NathDebasish Bhattacharyya
May 5, 2010·Proceedings of the National Academy of Sciences of the United States of America·Graham M WestMichael C Fitzgerald
Dec 23, 2003·European Journal of Biochemistry·Amrita Brahma, Debasish Bhattacharyya
Jul 5, 2001·Archives of Biochemistry and Biophysics·B Barat, D Bhattacharyya

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