Structural determinants of the stability of thermolysin-like proteinases.
Thermolysin is a member of a family of homologous proteinases which differ in their resistance to thermally induced unfolding and subsequent autolytic degradation. Site-directed mutagenesis studies of the thermolysin-like proteinase (TLP) from Bacillus stearothermophilus (TLP-ste) show that its reduced resistance to thermally induced autolysis, as compared to thermolysin, is due to only some of the 44 naturally occurring amino-acid differences between them. In fact TLP-ste becomes more resistant than thermolysin by mutation of just a few of these amino-acids. The crucial differences are all localized to a solvent-exposed region in the N-terminal domain of TLP-ste.
Eijsink
V G
VG
Department of Genetics, Center for Biological Sciences, University of Groningen, The Netherlands.
Veltman
O R
OR
Aukema
W
W
Vriend
G
G
Venema
G
G
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics; D006358:Hot Temperature; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009154:Mutation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D013820:Thermolysin / Q000737:chemistry* / Q000235:genetics
D010450:Endopeptidases; D013820:Thermolysin