PMID: 2124807Nov 15, 1990Paper

Identification of autodigestion target sites in Bacillus subtilis neutral proteinase

The Biochemical Journal
B van den BurgG Venema

Abstract

Autocatalytic degradation of purified Bacillus subtilis neutral proteinase was examined under various conditions. At elevated temperatures, under non-inhibitory conditions, mature protein was rapidly degraded, but no accumulation of specific breakdown products occurred. However, by incubating purified neutral proteinase on ice during extended periods of time, specific peptides accumulated. These peptides were analysed by SDS/PAGE and Western blotting, and the N-terminal sequences were determined for the four major peptides, which had sizes of 30, 22, 20 and 15 kDa. Sequence data identified five fission sites in the neutral proteinase, three of which were identical with autodigestion target sites in thermolysin, a thermostable neutral proteinase. Comparison of the identified fission sites of the B. subtilis neutral proteinase with the known substrate-specificity of the enzyme indicated that they were in agreement, showing a preference for the generation of fissions at the N-terminal side of large hydrophobic residues, such as leucine, isoleucine and methionine. These results suggest a high degree of similarity in the three-dimensional structures of B. subtilis neutral proteinase and thermolysin.

Citations

May 1, 1995·Nature Structural Biology·V G EijsinkG Venema
Mar 15, 1994·European Journal of Biochemistry·B Van den BurgV G Eijsink
Aug 1, 1993·Journal of Computer-aided Molecular Design·G Vriend, V Eijsink
Mar 1, 2006·International Journal of Behavioral Medicine·Richard PeterUNKNOWN SHEEP Study Group
Oct 4, 2002·International Journal of Behavioral Medicine·Gita D MishraPenny Warner-Smith
May 1, 1991·Journal of Biomolecular NMR·W EberleP Rösch
Apr 25, 1997·The Journal of Biological Chemistry·J MansfeldV G Eijsink
Dec 6, 2011·Applied Biochemistry and Biotechnology·Yoshiki MatsumiyaMotoki Kubo
Apr 16, 1998·Biochimica Et Biophysica Acta·S J Hubbard

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