1994年
SIGNAL PEPTIDASE CLEAVAGE SITE IN THE PROCESSING OF PSEUDOMONAS-AERUGINOSA PREPROELASTASE
JOURNAL OF FERMENTATION AND BIOENGINEERING
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- 巻
- 78
- 号
- 4
- 開始ページ
- 331
- 終了ページ
- 332
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/0922-338X(94)90367-0
- 出版者・発行元
- SOC FERMENTATION BIOENGINEERING, JAPAN
The extracellular elastase (33 kDa) of Pseudomonas aeruginosa is synthesized as a 53.6-kDa preproenzyme containing a long N-terminal propeptide, which is processed to the mature form via a 51-kDa proelastase. A 51-kDa protein isolated from Escherichia coli transformant carrying the Glu(141)-->Gln mutant elastase gene was subjected to N-terminal amino acid sequence analysis. No autoproteolytic processing of proelastase was expected to occur in these cells. The data indicated that the N-terminal sequence corresponds to the position between -174 and -164 of the preproelastase (numbers are in reference to the first amino acid residue of mature elastase). This confirms that the 51-kDa protein is proelastase and that the signal peptidase cleaves between Ala(-175) and Ala(-174).
- リンク情報
- ID情報
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- DOI : 10.1016/0922-338X(94)90367-0
- ISSN : 0922-338X
- Web of Science ID : WOS:A1994PP69200012