Comparative study on specificities of rat cathepsin L and papain: Amino acid differences at substrate-binding sites are involved in their specificities

Hironobu Koga, Hidenori Yamada, Yukio Nishimura, Keitaro Kato, Taiji Imoto

研究成果: ジャーナルへの寄稿記事

26 引用 (Scopus)

抄録

Sixty-nine rat cathepsin L-susceptible peptide bonds were analyzed employing various peptide substrates. The proteolytic specificities of rat cathepsin L and papain were compared and the results are discussed in relation to differences in amino acid residues around their binding sites. The specificity of cathepsin L, which is characterized by a remarkable preference for hydrophobic amino acids at the P2 site of the scissile peptide bonds, was analogous to that of papain as a whole. This analogous specificity suggests that the binding sites of the two proteases are analogous, as expected from their homologous amino acid sequences. However, there is a slight difference in the preference for S3 site between them. That is, cathepsin L showed a greater preference for bulky and hydrophobic amino acids at the S3 site than did papain. Based on the computer-graphically deduced structure of the binding sites of cathepsin L, the preferences for hydrophobic amino acids at the S2 site and for bulky and hydrophobic amino acids at the S3 site of the protease are supposed to be related to the compensating amino acid substitutions at the S2 site (V133A and V157L) and the reduction in size at the S3 site (Y61Q and Y67L), respectively. The discussion of the effect of the amino acid substitutions on the proteolytic activities of cathepsin L and papain in this paper provides a basis for more advanced studies of the relationship between structure and function of proteases belonging to the papain super-family by means of protein engineering.

元の言語英語
ページ(範囲)976-982
ページ数7
ジャーナルJournal of Biochemistry
108
発行部数6
DOI
出版物ステータス出版済み - 1 1 1990

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Papain
Cathepsin L
Binding Sites
Amino Acids
Substrates
Peptide Hydrolases
Amino Acid Substitution
Peptides
Protein Engineering
Amino Acid Sequence Homology
Substitution reactions
rat Ctsl protein

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Comparative study on specificities of rat cathepsin L and papain : Amino acid differences at substrate-binding sites are involved in their specificities. / Koga, Hironobu; Yamada, Hidenori; Nishimura, Yukio; Kato, Keitaro; Imoto, Taiji.

:: Journal of Biochemistry, 巻 108, 番号 6, 01.01.1990, p. 976-982.

研究成果: ジャーナルへの寄稿記事

Koga, Hironobu ; Yamada, Hidenori ; Nishimura, Yukio ; Kato, Keitaro ; Imoto, Taiji. / Comparative study on specificities of rat cathepsin L and papain : Amino acid differences at substrate-binding sites are involved in their specificities. :: Journal of Biochemistry. 1990 ; 巻 108, 番号 6. pp. 976-982.
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abstract = "Sixty-nine rat cathepsin L-susceptible peptide bonds were analyzed employing various peptide substrates. The proteolytic specificities of rat cathepsin L and papain were compared and the results are discussed in relation to differences in amino acid residues around their binding sites. The specificity of cathepsin L, which is characterized by a remarkable preference for hydrophobic amino acids at the P2 site of the scissile peptide bonds, was analogous to that of papain as a whole. This analogous specificity suggests that the binding sites of the two proteases are analogous, as expected from their homologous amino acid sequences. However, there is a slight difference in the preference for S3 site between them. That is, cathepsin L showed a greater preference for bulky and hydrophobic amino acids at the S3 site than did papain. Based on the computer-graphically deduced structure of the binding sites of cathepsin L, the preferences for hydrophobic amino acids at the S2 site and for bulky and hydrophobic amino acids at the S3 site of the protease are supposed to be related to the compensating amino acid substitutions at the S2 site (V133A and V157L) and the reduction in size at the S3 site (Y61Q and Y67L), respectively. The discussion of the effect of the amino acid substitutions on the proteolytic activities of cathepsin L and papain in this paper provides a basis for more advanced studies of the relationship between structure and function of proteases belonging to the papain super-family by means of protein engineering.",
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