Autolysis of a novel multidomain subtilase—cold-adapted deseasin MCP-01 is pH-dependent and the surface loops in its catalytic domain, the linker, and the P_proprotein domain are susceptible to proteolytic attack
- 8 May 2007
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 358 (3) , 704-709
- https://doi.org/10.1016/j.bbrc.2007.04.193
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- MEROPS: the peptidase databaseNucleic Acids Research, 2006
- The functional significance of the autolysis loop in protein C and activated protein CThrombosis and Haemostasis, 2005
- Autolysis of the Proteinase from Pseudomonas fluorescensJournal of Dairy Science, 1999
- Mechanism and kinetics of inactivation at 40–70°C of the extracellular proteinase from Pseudomonas fluorescens 22FJournal of Dairy Research, 1998
- Two Mutations in Rat Trypsin Confer Resistance against AutolysisBiochemical and Biophysical Research Communications, 1998
- Factors affecting autolysis of a subtilisin-like serine proteinase secreted by Ophiostoma piceae and identification of the cleavage siteBiochimica et Biophysica Acta (BBA) - General Subjects, 1995
- Autolysis and inhibition of proteinase K, a subtilisin-related serine proteinase isolated from the fungus Tritirachium album LimberBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Mechanisms of heat inactivation of a proteinase from Pseudomonas fluorescens biotype IJournal of Dairy Research, 1987
- Correlation between sites of limited proteolysis and segmental mobility in thermolysinBiochemistry, 1986
- Thermal stability of an extracellular proteinase fromPseudomonas fluorescensAFT 36Journal of Dairy Research, 1983