Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification.
cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue.
pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle.
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
Peptidyldiazomethanes. A novel mechanism of interaction with prolyl endopeptidase.
Unusual secondary specificity of prolyl oligopeptidase and the different reactivities of its two forms toward charged substrates.
Cleavage of the Lys196-Ser197 bond of prolyl oligopeptidase: enhanced catalytic activity for one of the two active enzyme forms.
Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine.
Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step.
New potent prolyl endopeptidase inhibitors: synthesis and structure-activity relationships of indan and tetralin derivatives and their analogues.
Synthesis and structure-activity relationships of peptidyl alpha-keto heterocycles as novel inhibitors of prolyl endopeptidase.
Benzyloxycarbonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine.
Probing substrate backbone function in prolyl oligopeptidase catalysis--large positional effects of peptide bond monothioxylation.
Low barrier hydrogen bond is absent in the catalytic triads in the ground state but Is present in a transition-state complex in the prolyl oligopeptidase family of serine proteases.
New fluorogenic substrates for the study of secondary specificity of prolyl oligopeptidase.
The specificity of prolyl endopeptidase from Flavobacterium meningoseptum: mapping the S' subsites by positional scanning via acyl transfer.
Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.
Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
Engineering cyclophilin into a proline-specific endopeptidase.
Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain.
Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.
Prolyl endopeptidase inhibitors from the underground part of Rhodiola sachalinensis.
Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue.
Trypanosoma cruzi prolyl oligopeptidase Tc80 is involved in nonphagocytic mammalian cell invasion by trypomastigotes.
Kinetic and mechanistic studies of prolyl oligopeptidase from the hyperthermophile Pyrococcus furiosus.
Substrate-dependent, non-hyperbolic kinetics of pig brain prolyl oligopeptidase and its tight binding inhibition by JTP-4819.
4-Phenylbutanoyl-2(S)-acylpyrrolidines and 4-phenylbutanoyl-L-prolyl-2(S)-acylpyrrolidines as prolyl oligopeptidase inhibitors.
Enzyme inhibitory constituents from Duranta repens.
Substrate recognition properties of oligopeptidase B from Salmonella enterica serovar Typhimurium.
Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site.
Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.
A prolyl endopeptidase-inhibiting benzofuran dimer from Polyozellus multiflex.
Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding.
Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.
This enzyme belongs to the peptidase family-S9A. According to the literature [22] & [29], this enzyme has got a catalytic triad (Ser554, Asp641, His680) as in the classical serine proteases such as trypsin. However, the oxyanion hole, which stabilizes the tetrahedral intermediate, is composed of the hydroxyl group of Tyr473 and mainchain amide group of Asn555 (see [29]).