Structural and Catalytic Roles of the Disulfide Bonds Cys19–Cys154 and Cys134–Cys199 in Trypsin-like Proteases: Evolutionary Insights for Disulfide Bond Acquisition

Trypsin is one of the most extensively studied enzymes in biochemistry. However, little information is available on the role of the disulfide bonds to establish the correct conformation and enzyme activity during molecular evolution. To obtain this information, two additional disulfide bonds corresp...

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Hlavní autoři:	Maiko Minakata, Yuri Murakami, Orika Ashida, Miki Matsuzaki, Kairi Ogawa, Nanako Saeki, Shigeru Shimamoto, Mitsuhiro Miyazawa, Yuji Hidaka, Nana Sakata
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	MDPI AG 2026-01-01
Edice:	Molecules
Témata:	denaturation disulfide folding molecular evolution mutation
On-line přístup:	https://www.mdpi.com/1420-3049/31/2/351
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