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Structural Characterization Reveals the Keratinolytic Activity of an Arthrobacter nicotinovorans Protease
Title: | Structural Characterization Reveals the Keratinolytic Activity of an Arthrobacter nicotinovorans Protease |
Authors: | Sone, Teruo Browse this author →KAKEN DB | Haraguchi, Yumiko Browse this author | Kuwahara, Aki Browse this author | Ose, Toyoyuki Browse this author →KAKEN DB | Takano, Megumi Browse this author | Abe, Ayumi Browse this author | Tanaka, Michiko Browse this author | Tanaka, Isao Browse this author →KAKEN DB | Asano, Kozo Browse this author →KAKEN DB |
Keywords: | Arthrobacter nicotinovorans | cadmium | crystallization | metallothionein | scallops | serine protease |
Issue Date: | Jan-2015 |
Publisher: | Bentham Science Publishers |
Journal Title: | Protein and peptide letters |
Volume: | 22 |
Issue: | 1 |
Start Page: | 63 |
End Page: | 72 |
Publisher DOI: | 10.2174/0929866521666140919100851 |
Abstract: | Elevated cadmium (Cd) concentrations in fishery byproducts are an environmental concern, that might be reduced by enzymatic removal and adsorption of the contaminants during recycling the byproducts as animal food. We cloned the gene for Arthrobacter nicotinovorans serine protease (ANISEP), which was isolated from the hepatopancreas of the Japanese scallop (Patiopecten yessoensis) and has been found to be an effective enzyme for Cd(II) removal. The gene is 993 bp in length and encodes 330 amino acids, including the pre (1-30) and pro (31-111) sequences. The catalytic triad consists of His, Asp, and Ser. Sequence similarities indicate that ANISEP is a extracellular serine protease. X-ray crystallography revealed structural similarities between ANISEP and the trypsin-like serine protease NAALP from Nesterenkonia sp. Site-directed mutagenesis identified Ser171 as catalytic residue. The keratinolytic activity of ANISEP was 10-fold greater than that of trypsin. ANISEP digested Cd(II)-bound recombinant metallothionein MT-10a from Laternula elliptica, but did not release Cd. These results further suggest ANISEP is a trypsin-like serine protease that can release Cd from the Japanese scallop hepatopancreas because of its strong keratinolytic activity. |
Rights: | The published manuscript is available at EurekaSelect via http://www.eurekaselect.com/openurl/content.php?genre=article&doi=10.2174/0929866521666140919100851. |
Relation: | http://benthamscience.com/index.php |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/60612 |
Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 曾根 輝雄
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