Journal
IUBMB LIFE
Volume 61, Issue 5, Pages 510-515Publisher
JOHN WILEY & SONS INC
DOI: 10.1002/iub.186
Keywords
serine proteases; enzyme catalysis; thrombin; allostery
Categories
Funding
- NIH [HL49413, HL58141, HL73813]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL049413, R01HL058141, R01HL073813, R29HL049413] Funding Source: NIH RePORTER
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Over one third of all known proteolytic enzymes are serine proteases. Among these, the trypsins underwent the most predominant genetic expansion yielding the enzymes responsible for digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis. and immunity. The success of this expansion resides in it highly efficient fold that couples catalysis and regulatory interactions. Added complexity comes front the recent observation of it significant conformational plasticity of the trypsin fold. A new paradigm emerges where two forms of, the protease, E* and E, are in allosteric equilibrium and determine biological activity and specificity. (C) 2009 IUBMB IUBMB Life, 61(5): 510-515, 2009
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