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Carboxypeptidase Z(CPZ) cDNA of Absidia zychae was experssed in Saccharomyces cerevisiae. The expressed CPZ(YCPZ) was secreted about 30 mg/l into the medium and has a little higher molecular weight than the wild type CPZ in SDS-PAGE. By the result of N-terminal amino acid sequencing, YCPZ has additional 15 amino acids residues in N-terminus of CPZ. But YCPZ shows no difference with CPZ in enzyme activity and substrate specificity. For the identification of processing mechanism of YCPZ, 36-Arg was changed to 36-Thr by site specific mutagenesis. Mutant YCPZ does not processed at 36-Thr. It was, therefore, concluded that the YCPZ was processed by KEX2. According to endo F treatment, high amount of carbohydrate was N-glycosylated in YCPZ.
Keywords: Carboxypeptidase Z. Saccharomyces cerevisiae, Absidia zychae, KEX2, processing, glycosylation, cDNA, site specific mutagenesis
Yinuo Fei, Yan Shao, Weiwei Wang, Yatian Cheng, Boyang Yu, Xiaorong He*, and Jian Zhang*Microbiol. Biotechnol. Lett. 2021; 49(2): 174-180 https://doi.org/10.48022/mbl.2012.02010
신동하, 김재범, 김병우, 남수완, 신지원, 정대균, 정춘수Microbiol. Biotechnol. Lett. 1998; 26(5): 406-412 https://doi.org/10.4014/mbl.19188.8.131.526