2002年8月
The role of the N-terminal propeptide of the pro-aminopeptidase processing protease: refolding, processing, and enzyme inhibition
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- ,
- ,
- ,
- 巻
- 296
- 号
- 1
- 開始ページ
- 78
- 終了ページ
- 84
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/S0006-291X(02)00838-0
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
Pro-aminopeptidase processing protease (PA protease) is an extracellular zinc metalloprotease produced by Aeromonas caviae T-64 and it is classified as M04.016 according to the MEROPS database. The precursor of PA protease consists of four regions; a signal peptide, an N-terminal propeptide, a C-terminal propeptide, and the mature PA protease. The in vitro refolding of the intermediate pro-PA protease containing the C-terminal propeptide (MC) was investigated in the presence and absence of the N-terminal propeptide. The results indicate that the noncovalently linked N-terminal propeptide is able to assist in the refolding of MC. In the absence of the N-terminal propeptide, MC is trapped into a folding competent state that is converted into the active form by the addition of the N-terminal propeptide. Moreover, the N-terminal propeptide was found to form a complex with the folded MC and inhibit further processing of MC into the mature PA protease. Inhibitory activity of the purified N-terminal propeptide toward mature PA protease was also observed, and the mode of this inhibition was determined to be a mixed, noncompetitive inhibition with an associated allosteric effect. (C) 2002 Elsevier Science (USA). All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/S0006-291X(02)00838-0
- ISSN : 0006-291X
- PubMed ID : 12147230
- Web of Science ID : WOS:000177525700014