Literature DB >> 12162566

Increased proteolytic susceptibility of carboxypeptidase Y caused by modification of the disulfide zipper.

Toshihiko Maki1, Hajime Kozawa, Joji Mima, Hiroshi Ueno, Rikimaru Hayashi.   

Abstract

To investigate the structural importance of a "disulfide zipper" motif of carboxypeptidase Y, disulfide-deficient mutant enzymes were expressed in two strains of Saccharomyces cerevisiae. The mutant enzymes were rapidly degraded into fragments by intracellular proteases. Thus, it is concluded that the disulfide zipper is essential in maintaining the structural integrity of CPase Y against proteolytic susceptibility.

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Year:  2002        PMID: 12162566     DOI: 10.1271/bbb.66.1393

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  1 in total

1.  Carboxypeptidase Y activity and maintenance is modulated by a large helical structure.

Authors:  Mai Makino; Takehiko Sahara; Naoki Morita; Hiroshi Ueno
Journal:  FEBS Open Bio       Date:  2019-06-17       Impact factor: 2.693

  1 in total

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