Inter-molecular degradation of signal peptidase I in vitro

Clicks: 179
ID: 267920
1991
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Abstract
Highly purified preparations of signal peptidase I (36 kDa) were found to undergo an apparent inter-autocatalytic degradation at 4°C and 37° C. The disappearance of the 36 kDa protein coincided with the stable appearance of a 31 kDa and a 5 kDa species. Amino-terminal sequencing of the 31 kDa product indicated a site specific cleavage following Ala38-Gln-Ala of signal peptidase I. The 31 kDa fragment was purified and shown to have 100-fold less activity than the native enzyme, with pre-maltose binding protein as a substrate.
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Authors Todd L. Talarico,Inderjit K. Dev,Philip J. Bassford,Paul H. Ray;Todd L. Talarico;Inderjit K. Dev;Philip J. Bassford;Paul H. Ray;
Journal Biochemical and biophysical research communications
Year 1991
DOI
10.1016/0006-291x(91)91240-d
URL
https://sciprofiles.com/publication/view/7be0e1ce1fc4048f9da6aa8e0cf117a2
Keywords
protein purified fold cleavage signal peptidase terminal gln autocatalytic

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