TY - JOUR
T1 - Autoproteolytic stability of a trypsin from the marine crab Cancer pagurus
AU - Hehemann, Jan Hendrik
AU - Redecke, Lars
AU - Murugaiyan, Jayaseelan
AU - von Bergen, Martin
AU - Betzel, Christian
AU - Saborowski, Reinhard
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2008/6/13
Y1 - 2008/6/13
N2 - Autoproteolytic stability is a crucial factor for the application of proteases in biotechnology. In contrast to vertebrate enzymes, trypsins from shrimp and crayfish are known to be resistant against autolysis. We show by characterisation of a novel trypsin from the gastric fluid of the marine crab Cancer pagurus that this property might be assigned to the entire class of crustaceans. The isolated and cloned crab trypsin (C.p.TryIII) exhibits all characteristic properties of crustacean trypsins. However, its overall sequence identity to other trypsins of this systematic class is comparatively low. The high resistance against autoproteolysis was determined by mass spectrometry, which revealed a low susceptibility of the N-terminal domain towards autolysis. By homology modelling of the tertiary structure, the elevated stability was attributed to the distinctly different pattern of autolytic cleavage sites, which is conserved in all known crustacean trypsin sequences.
AB - Autoproteolytic stability is a crucial factor for the application of proteases in biotechnology. In contrast to vertebrate enzymes, trypsins from shrimp and crayfish are known to be resistant against autolysis. We show by characterisation of a novel trypsin from the gastric fluid of the marine crab Cancer pagurus that this property might be assigned to the entire class of crustaceans. The isolated and cloned crab trypsin (C.p.TryIII) exhibits all characteristic properties of crustacean trypsins. However, its overall sequence identity to other trypsins of this systematic class is comparatively low. The high resistance against autoproteolysis was determined by mass spectrometry, which revealed a low susceptibility of the N-terminal domain towards autolysis. By homology modelling of the tertiary structure, the elevated stability was attributed to the distinctly different pattern of autolytic cleavage sites, which is conserved in all known crustacean trypsin sequences.
UR - http://www.scopus.com/inward/record.url?scp=43049139443&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2008.03.128
DO - 10.1016/j.bbrc.2008.03.128
M3 - Journal articles
C2 - 18395521
AN - SCOPUS:43049139443
SN - 0006-291X
VL - 370
SP - 566
EP - 571
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -
