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Literature summary for 3.4.16.5 extracted from

  • Winther, J.R.; Sorensen, P.; Kielland-Brandt, M.C.
    Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion (1994), J. Biol. Chem., 269, 22007-22013.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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carboxypeptidase Y
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Renatured (Commentary)

Renatured (Comment) Organism
efficient folding of carboxypeptidase Y is dependent on the presence of the proregion. Thus denatured pro-carboxypeptidase Y, in contrast to the mature enzyme, refolds efficiently in vitro in low ionic strength buffers. Under these conditions denatured mature carboxypeptidase Y forms an inactive, soluble folding intermediate Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation expressed in Escherichia coli Saccharomyces cerevisiae
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