Increased proteolytic susceptibility of carboxypeptidase Y caused by modification of the disulfide zipper.
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.
Maki
Toshihiko
T
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.
Kozawa
Hajime
H
Mima
Joji
J
Ueno
Hiroshi
H
Hayashi
Rikimaru
R
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
D004220:Disulfides; D002268:Carboxypeptidases; D010450:Endopeptidases; D043402:Cathepsin A