Increased Proteolytic Susceptibility of Carboxypeptidase Y Caused by Modification of the Disulfide Zipper | Zendy

Toshihiko Maki | Zendy; Hajime KOZAWA | Zendy; Joji Mima | Zendy; Hiroshi Ueno | Zendy; Rikimaru Hayashi | Zendy

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Increased Proteolytic Susceptibility of Carboxypeptidase Y Caused by Modification of the Disulfide Zipper

Author(s) -

Toshihiko Maki,

Hajime KOZAWA,

Joji Mima,

Hiroshi Ueno,

Rikimaru Hayashi

Publication year - 2002

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.66.1393

Subject(s) - zipper , carboxypeptidase , proteases , chemistry , disulfide bond , biochemistry , mutant , cysteine , enzyme , proteolytic enzymes , protein disulfide isomerase , gene , algorithm , computer science

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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