Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume 1122, Issue 3, 21 August 1992, Pages 283-292
A heat-stable serine proteinase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
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Archaean Serine Proteases
2013, Handbook of Proteolytic EnzymesKinetic and Mechanistic Studies of Prolyl Oligopeptidase from the Hyperthermophile Pyrococcus furiosus
2001, Journal of Biological ChemistryCitation Excerpt :This contention is also supported by the AEBSF inhibition study and heat of ionization, which both suggest that Ser-477 is activated by the ionization of the imidazole from His-592. The ionization of pK 1 for Pfu POP has some unusual characteristics compared with most serine proteases; however, similar observations have been made for thermophilic proteases (36, 37) and another POP (38). Fig. 4 shows that a high percentage of the enzyme activity is dependent upon the ionization of the first ionizable group with a pK a at ∼4.0–4.7 depending on the ionic strength.
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Copyright © 1992 Published by Elsevier B.V.