Propeptide-mediated protein folding: mechanism and its impact on lipase.

Miao Tian; Jun Zhang; Wen Luo; Zhiyuan Wang; Junying FU; Shaowei Huang; Pengmei LÜ

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Propeptide-mediated protein folding: mechanism and its impact on lipase.

Author: Miao TIAN ¹ ; Jun ZHANG ¹ ; Wen LUO ¹ ; Zhiyuan WANG ¹ ; Junying FU ¹ ; Shaowei HUANG ² ; Pengmei LÜ ¹
Author Information

1. Key Laboratory of Renewable Energy, Guangzhou Institute of Energy Conversion, Chinese Academy of Sciences, Guangzhou 510640, Guangdong, China.
2. College of Forestry and Landscape Architecture, South China Agricultural University, Guangzhou 510642, Guangdong, China.
Publication Type:Journal Article
Keywords: disulfide bond; folding mechanism; glycosylation; lipase; propeptide
MeSH: Lipase/metabolism*; Molecular Chaperones/metabolism*; Protein Folding; Protein Precursors; Substrate Specificity
From: Chinese Journal of Biotechnology 2021;37(1):88-99
CountryChina
Language:Chinese
Abstract: The formation of most proteins consists of two steps: the synthesis of precursor proteins and the synthesis of functional proteins. In these processes, propeptides play important roles in assisting protein folding or inhibiting its activity. As an important polypeptide chain coded by a gene sequence in lipase gene, propeptide usually functions as an intramolecular chaperone, assisting enzyme molecule folding. Meanwhile, some specific sites on propeptide such as glycosylated sites, have important effect on the activity, stability in extreme environment, methanol resistance and the substrate specificity of the lipase. Studying the mechanism of propeptide-mediated protein folding, as well as the influence of propeptide on lipases, will allow to regulate lipase by alternating the propeptide folding behavior and in turn pave new ways for protein engineering research.