Structural Characterization Reveals the Keratinolytic Activity of an Arthrobacter nicotinovorans Protease

Sone, Teruo; Haraguchi, Yumiko; Kuwahara, Aki; Ose, Toyoyuki; Takano, Megumi; Abe, Ayumi; Tanaka, Michiko; Tanaka, Isao; Asano, Kozo

Structural Characterization Reveals the Keratinolytic Activity of an Arthrobacter nicotinovorans Protease

Sone, Teruo; Haraguchi, Yumiko; Kuwahara, Aki et al.

Protein and peptide letters, 2015, 22(1), 63-72

Permalink : https://hdl.handle.net/2115/60612

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アクセス権	open access
URI	https://hdl.handle.net/2115/60612
タイトル	Structural Characterization Reveals the Keratinolytic Activity of an Arthrobacter nicotinovorans Protease
著者	Sone, Teruo ; Haraguchi, Yumiko ; Kuwahara, Aki ; Ose, Toyoyuki ; Takano, Megumi ; Abe, Ayumi ; Tanaka, Michiko ; Tanaka, Isao ; Asano, Kozo
e-Rad_Researcher 00333633 著者名 Sone, Teruo
著者名 Haraguchi, Yumiko
著者名 Kuwahara, Aki
e-Rad_Researcher 80380525 著者名 Ose, Toyoyuki
著者名 Takano, Megumi
著者名 Abe, Ayumi
著者名 Tanaka, Michiko
e-Rad_Researcher 70093052 著者名 Tanaka, Isao
e-Rad_Researcher 50312393 著者名 Asano, Kozo
言語	英語
キーワード	Arthrobacter nicotinovorans
	cadmium
	crystallization
	metallothionein
	scallops
	serine protease
発行日	2015-01
出版者	Bentham Science Publishers
収録物名	Protein and peptide letters
巻(号)	22(1)
ページ	63-72
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	The published manuscript is available at EurekaSelect via http://www.eurekaselect.com/openurl/content.php?genre=article&doi=10.2174/0929866521666140919100851.
PISSN	0929-8665
関連情報	URI http://benthamscience.com/index.php
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.2174/0929866521666140919100851