title: Increased proteolytic susceptibility of carboxypeptidase Y caused by modification of the disulfide zipper.
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.
authors.affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Maki
authors.forename: Hajime
authors.initials: H
authors.lastname: Kozawa
authors.forename: Joji
authors.initials: J
authors.lastname: Mima
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Ueno
authors.forename: Rikimaru
authors.initials: R
authors.lastname: Hayashi
mesh_terms: D015153:Blotting, Western; D002268:Carboxypeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D043402:Cathepsin A; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D004795:Enzyme Stability; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics
chemical_list: D004220:Disulfides; D002268:Carboxypeptidases; D010450:Endopeptidases; D043402:Cathepsin A