Endo- and Aminopeptidase Activities of Rat Cathepsin H

Hironobu Koga, Nobuko Mori, Hidenori Yamada, Yukio Nishimura, Kazuo Tokuda, Keitaro Kato, T. Taiji

研究成果: ジャーナルへの寄稿記事

35 引用 (Scopus)

抄録

Employing soluble denatured protein substrates and their derivatives, the proteolytic activity of rat cathepsin H was investigated. The enzyme showed aminopeptidase activity which sequentially released amino acid from the N-terminal of the substrate. The aminopeptidase activity did not act on Na-acetylated peptides and showed moderate ionic-strength dependence when methionyl-methylcoumarylamide was employed as a substrate. These results indicate that the activity essentially requires an N-terminal free amino group of the substrate and recognizes it electrostatically to some extent. On the other hand, the enzyme was also indicated to exhibit endopeptidase activity by employing appropriate Na-acetylated peptide substrates. In contrast to the aminopeptidase activity, the endopeptidase activity showed rather strict specificity, preferring hydrophobic residues at P2 and P3 sites. Because of the broad specificity and high efficiency of the aminopeptidase activity, it was difficult to directly observe endopeptidase activity in the digestion of large peptide substrates with a free a-amino terminal. Thus, this is the first experimental evidence that indicates endopeptidase activity by assigning internal peptide bonds cleaved by this activity. From this data, we proposed a model of the binding site of this enzyme.

元の言語英語
ページ(範囲)965-970
ページ数6
ジャーナルChemical and Pharmaceutical Bulletin
40
発行部数4
DOI
出版物ステータス出版済み - 1 1 1992

Fingerprint

Cathepsin H
Endopeptidases
Aminopeptidases
Rats
Peptides
Substrates
Enzymes
Osmolar Concentration
Digestion
Binding Sites
Ionic strength
Amino Acids
Derivatives
Proteins

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Drug Discovery

これを引用

Koga, H., Mori, N., Yamada, H., Nishimura, Y., Tokuda, K., Kato, K., & Taiji, T. (1992). Endo- and Aminopeptidase Activities of Rat Cathepsin H. Chemical and Pharmaceutical Bulletin, 40(4), 965-970. https://doi.org/10.1248/cpb.40.965

Endo- and Aminopeptidase Activities of Rat Cathepsin H. / Koga, Hironobu; Mori, Nobuko; Yamada, Hidenori; Nishimura, Yukio; Tokuda, Kazuo; Kato, Keitaro; Taiji, T.

:: Chemical and Pharmaceutical Bulletin, 巻 40, 番号 4, 01.01.1992, p. 965-970.

研究成果: ジャーナルへの寄稿記事

Koga, H, Mori, N, Yamada, H, Nishimura, Y, Tokuda, K, Kato, K & Taiji, T 1992, 'Endo- and Aminopeptidase Activities of Rat Cathepsin H', Chemical and Pharmaceutical Bulletin, 巻. 40, 番号 4, pp. 965-970. https://doi.org/10.1248/cpb.40.965
Koga H, Mori N, Yamada H, Nishimura Y, Tokuda K, Kato K その他. Endo- and Aminopeptidase Activities of Rat Cathepsin H. Chemical and Pharmaceutical Bulletin. 1992 1 1;40(4):965-970. https://doi.org/10.1248/cpb.40.965
Koga, Hironobu ; Mori, Nobuko ; Yamada, Hidenori ; Nishimura, Yukio ; Tokuda, Kazuo ; Kato, Keitaro ; Taiji, T. / Endo- and Aminopeptidase Activities of Rat Cathepsin H. :: Chemical and Pharmaceutical Bulletin. 1992 ; 巻 40, 番号 4. pp. 965-970.
@article{543a755afdc1412598896423e5b37623,
title = "Endo- and Aminopeptidase Activities of Rat Cathepsin H",
abstract = "Employing soluble denatured protein substrates and their derivatives, the proteolytic activity of rat cathepsin H was investigated. The enzyme showed aminopeptidase activity which sequentially released amino acid from the N-terminal of the substrate. The aminopeptidase activity did not act on Na-acetylated peptides and showed moderate ionic-strength dependence when methionyl-methylcoumarylamide was employed as a substrate. These results indicate that the activity essentially requires an N-terminal free amino group of the substrate and recognizes it electrostatically to some extent. On the other hand, the enzyme was also indicated to exhibit endopeptidase activity by employing appropriate Na-acetylated peptide substrates. In contrast to the aminopeptidase activity, the endopeptidase activity showed rather strict specificity, preferring hydrophobic residues at P2 and P3 sites. Because of the broad specificity and high efficiency of the aminopeptidase activity, it was difficult to directly observe endopeptidase activity in the digestion of large peptide substrates with a free a-amino terminal. Thus, this is the first experimental evidence that indicates endopeptidase activity by assigning internal peptide bonds cleaved by this activity. From this data, we proposed a model of the binding site of this enzyme.",
author = "Hironobu Koga and Nobuko Mori and Hidenori Yamada and Yukio Nishimura and Kazuo Tokuda and Keitaro Kato and T. Taiji",
year = "1992",
month = "1",
day = "1",
doi = "10.1248/cpb.40.965",
language = "English",
volume = "40",
pages = "965--970",
journal = "Chemical and Pharmaceutical Bulletin",
issn = "0009-2363",
publisher = "The Pharmaceutical Society of Japan",
number = "4",

}

TY - JOUR

T1 - Endo- and Aminopeptidase Activities of Rat Cathepsin H

AU - Koga, Hironobu

AU - Mori, Nobuko

AU - Yamada, Hidenori

AU - Nishimura, Yukio

AU - Tokuda, Kazuo

AU - Kato, Keitaro

AU - Taiji, T.

PY - 1992/1/1

Y1 - 1992/1/1

N2 - Employing soluble denatured protein substrates and their derivatives, the proteolytic activity of rat cathepsin H was investigated. The enzyme showed aminopeptidase activity which sequentially released amino acid from the N-terminal of the substrate. The aminopeptidase activity did not act on Na-acetylated peptides and showed moderate ionic-strength dependence when methionyl-methylcoumarylamide was employed as a substrate. These results indicate that the activity essentially requires an N-terminal free amino group of the substrate and recognizes it electrostatically to some extent. On the other hand, the enzyme was also indicated to exhibit endopeptidase activity by employing appropriate Na-acetylated peptide substrates. In contrast to the aminopeptidase activity, the endopeptidase activity showed rather strict specificity, preferring hydrophobic residues at P2 and P3 sites. Because of the broad specificity and high efficiency of the aminopeptidase activity, it was difficult to directly observe endopeptidase activity in the digestion of large peptide substrates with a free a-amino terminal. Thus, this is the first experimental evidence that indicates endopeptidase activity by assigning internal peptide bonds cleaved by this activity. From this data, we proposed a model of the binding site of this enzyme.

AB - Employing soluble denatured protein substrates and their derivatives, the proteolytic activity of rat cathepsin H was investigated. The enzyme showed aminopeptidase activity which sequentially released amino acid from the N-terminal of the substrate. The aminopeptidase activity did not act on Na-acetylated peptides and showed moderate ionic-strength dependence when methionyl-methylcoumarylamide was employed as a substrate. These results indicate that the activity essentially requires an N-terminal free amino group of the substrate and recognizes it electrostatically to some extent. On the other hand, the enzyme was also indicated to exhibit endopeptidase activity by employing appropriate Na-acetylated peptide substrates. In contrast to the aminopeptidase activity, the endopeptidase activity showed rather strict specificity, preferring hydrophobic residues at P2 and P3 sites. Because of the broad specificity and high efficiency of the aminopeptidase activity, it was difficult to directly observe endopeptidase activity in the digestion of large peptide substrates with a free a-amino terminal. Thus, this is the first experimental evidence that indicates endopeptidase activity by assigning internal peptide bonds cleaved by this activity. From this data, we proposed a model of the binding site of this enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0026718934&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026718934&partnerID=8YFLogxK

U2 - 10.1248/cpb.40.965

DO - 10.1248/cpb.40.965

M3 - Article

C2 - 1525952

AN - SCOPUS:0026718934

VL - 40

SP - 965

EP - 970

JO - Chemical and Pharmaceutical Bulletin

JF - Chemical and Pharmaceutical Bulletin

SN - 0009-2363

IS - 4

ER -