Prolyl oligopeptidase from porcine brain, S554A mutant with bound peptide ligand GLY-PHE-ARG-PRO

Electrostatic Environment at the Active Site of Prolyl Oligopeptidase is Highly Influential During Substrate Binding

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

Structures of Prolyl Oligopeptidase Substrate/ Inhibitor Complexes. Use of Inhibitor Binding for Titration of the Catalytic Histidine Residue

Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism

Prolyl Oligopeptidase: An Unusual Beta-Propeller Domain Regulates Proteolysis

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH INHIBITOR

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH PEPTIDE

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND SUC- GLY-PRO

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC- GLY-PRO

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641N MUTANT WITH BOUND PEPTIDE LIGAND SUC- GLY-PRO

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU- PHE-SER-PRO

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

CLEAVES PEPTIDE BONDS ON THE C-TERMINAL SIDE OF PROLYL
RESIDUES WITHIN PEPTIDES OF UP TO APPROXIMATELY 30 AMINO
ACIDS IN LENGTH. BELONGS TO PEPTIDASE FAMILY S9A.

CATALYTIC ACTIVITY: HYDROLYSIS OF PRO-|-XAA >> ALA-|-XAA IN
OLIGOPEPTIDES.

ENGINEERED MUTATION IN CHAIN A, SER 554 ALA

THE MUTATED REGION CORREPONDS TO THE ACT_SITE CHARGE RELAY
OF THE SEQUENCE

PROLYL ENDOPEPTIDASE (E.C.3.4.21.26), PEPTIDE LIGAND GLY-PHE-ARG-PRO

THE DIMERIC ASSEMBLY DESCRIBED HERE IS DUE
TO A COMPLEXOF THE PROTEIN CHAIN A WITH A
PEPTIDE (CHAIN B). CHAIN A IS ESSENTIALLY A MONOMER
IN THE PHYSIOLOGICAL STATE.

HYDROLASE, PROLYL OLIGOPEPTIDASE, AMNESIA, ALPHA/ BETA-HYDROLASE, BETA-PROPELLER, SERINE PROTEASE