Multiple proteolytic action of rat liver cathepsin B: Specificities and pH-dependences of the endo- and exopeptidase activities

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

35 引用 (Scopus)

抄録

Dipeptidylcarboxypeptidase, endopeptidase, and carboxypeptidase activities of rat liver cathepsin B were investigated using soluble denatured protein substrates, reduced and S-(3-trimethylammonio)propylated proteins and their derivatives. It was found that the soluble denatured proteins were degraded mainly by the dipeptidylcarboxypeptidase activity and in a few cases by the endopeptidase and carboxypeptidase activities. The dipeptidylcarboxypeptidase activity showed broad substrate specificity with broad pH optimum at 4-6. A peptide having the α-carboxyl group amidated with methylamine could also be a good substrate for this activity. These results suggest that this activity is dependent not upon the dissociated α-carboxyl group at the P2' site but upon the hydrogen-bonding abilities of the α-imino moiety and the protonated or amidated α-carboxyl moiety at P2'. On the other hand, the endopeptidase and carboxypeptidase activities were observed in a few cases, suggesting that special amino acid sequences in the substrates are responsible for these activities. These activities showed sharp pH optima at 6 and seemed to prefer basic amino acid residues at P1 site. Therefore, we suppose that cathepsin B has a carboxyl group with a pKa, of about 5.5 at the S1 subsite which more effectively interacts with a positive charge at the P1 site of the substrate at pH 6 than at pH 5. Based on these results, a model of the binding subsites of this enzyme is proposed.

元の言語英語
ページ(範囲)179-188
ページ数10
ジャーナルJournal of Biochemistry
110
発行部数2
DOI
出版物ステータス出版済み - 1 1 1991

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Exopeptidases
Endopeptidases
Cathepsin B
Carboxypeptidases
Liver
Rats
Substrates
Basic Amino Acids
Proteins
Hydrogen Bonding
Substrate Specificity
Amino Acid Sequence
Hydrogen bonds
Peptides
Derivatives
Enzymes
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Multiple proteolytic action of rat liver cathepsin B : Specificities and pH-dependences of the endo- and exopeptidase activities. / Koga, Hironobu; Yamada, Hidenori; Nishimura, Yukio; Kato, Keitaro; Imoto, Taiji.

:: Journal of Biochemistry, 巻 110, 番号 2, 01.01.1991, p. 179-188.

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. / Multiple proteolytic action of rat liver cathepsin B : Specificities and pH-dependences of the endo- and exopeptidase activities. :: Journal of Biochemistry. 1991 ; 巻 110, 番号 2. pp. 179-188.
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