pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle.

  title={pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle.},
  author={László Polgár},
  journal={European journal of biochemistry},
  volume={197 2},
  • L. Polgár
  • Published 1991
  • Chemistry, Medicine
  • European journal of biochemistry
Prolyl endopeptidase, an enzyme exhibiting high specificity towards the Pro-Xaa bond, is thought to play an important role in the metabolism of biologically active peptides. (a) It has been found that pig muscle is an appropriate source for the preparation of a reasonable quantity of enzyme. Thus, 1 kg muscle yields 1-1.5 mg enzyme, homogeneous by fast protein liquid chromatography. (b) Bulky reagents reacting with cysteine residues inactivate the enzyme almost completely, whereas the small… Expand
Cleavage of the Lys196-Ser197 bond of prolyl oligopeptidase: enhanced catalytic activity for one of the two active enzyme forms.
The digestion experiments suggested that alteration in the ionic strength elicits conformational changes in native prolyl oligopeptidase, and this may account for the enhanced catalytic activity observed at higher ionsic strength. Expand
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Structure determination of the inactive S554A variant of prolyl oligopeptidase complexed with an octapeptide has shown that substrate binding is restricted to the P4-P2′ region. In addition, it hasExpand
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Kinetic and Mechanistic Studies of Prolyl Oligopeptidase from the Hyperthermophile Pyrococcus furiosus *
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Substrate-dependent, non-hyperbolic kinetics of pig brain prolyl oligopeptidase and its tight binding inhibition by JTP-4819.
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Chapter 3 Structure and function of serine proteases
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The proteases involved in the maturation of regulatory peptides like those of broader specificity normally fail to cleave peptide bonds linked to the cyclic amino acid proline, but in certain non‐mammalian tissues repetitive pre‐sequences of this type are removed by specialized dipeptidyl (amino) peptidases during maturation. Expand
The intrinsic pKa-values of functional groups in enzymes: improper deductions from the pH-dependence of steady-state parameters.
  • J. Knowles
  • Chemistry, Medicine
  • CRC critical reviews in biochemistry
  • 1976
The assumptions implicit in the deductions made from the pH-dependence of rate measurements of enzyme-catalyzed reactions are summarized, and the limitations of such determinations are discussedExpand
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Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four majorExpand