Shimba N

References (1)

Title : Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2 - Kodama_2009_Proteins_77_710
Author(s) : Kodama Y , Masaki K , Kondo H , Suzuki M , Tsuda S , Nagura T , Shimba N , Suzuki E , Iefuji H
Ref : Proteins , 77 :710 , 2009
Abstract : 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 A 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.
ESTHER : Kodama_2009_Proteins_77_710
PubMedSearch : Kodama_2009_Proteins_77_710
PubMedID: 19544571
Gene_locus related to this paper: crysp-Q874E9