期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 77, 期 3, 页码 710-717出版社
WILEY
DOI: 10.1002/prot.22484
关键词
CLE; lipase; cutinase; substrate specificity; hydrolysis; site-directed mutagenesis; protein engineering; structural biology
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
The structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 angstrom resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity. Proteins 2009; 77:710-717 (C) 2009 Wiley-Liss, Inc.
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