Substrate Specificity of a Novel Serine Protease from Soybean (Glycine max (L.) Merrill).

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概要

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• The substrate specificity of a novel serine protease isolated from soybean seeds, cultivar Keburi, was investigated using various peptide-MCAs and several neuropeptides involving single and paired basic amino acid sequences. The protease was quite specific for arginine residue at the P1 site of the active center, and it recognized paired Arg-Arg and cleaved at the linkage between Arg-Arg or after Arg-Arg in peptide and protein molecules. This is the first protease in plant tissues which resembles in substrate specificity the arginine-specific serine proteinases from porcine gastric and intestinal mucosa, recognizing paired basic amino acid sequences.

• 社団法人 日本生化学会の論文

著者

• MORITA Shimpei

  Central Research Institute, Fuji Oil Co.

• MORITA Yuhei

  Central Research Institute, Fuji Oil Co.

• YAMAGUCHI Masami

  Central Research Institute, Fuji Oil Co.

• Fukase Masami

  Central Research Institute Fuji Oil Co.

関連論文

• Thermal Stability of Individual Molecular Species of Soybean β-Conglycinin
• Substrate Specificity of a Novel Serine Protease from Soybean [Glycine max (L.) Merrill]
• Purification, Characterization, and Crystallization of Single Molecular Species of β-Conglycinin from Soybean Seeds
• Partial Purification and Characterization of a Novel Soybean Protease Which Is Inhibited by Kunitz and Bowman-Birk Trypsin Inbititors
• A Serine Protease in Soybean Seeds That Acts Specifically on the Native α Subunit of β-Conglycinin : PROTEINS, ENZYMES AND METABOLISM
• The Crystal Structure of Lipase II from Rhizopus niveus at 2.2 Å Resolution
• Purification, Characterization, and Crystallization of Two Types of Lipase from Rhizopus niveus
• Substrate Specificity of a Novel Serine Protease from Soybean (Glycine max (L.) Merrill).

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