Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
Mass-weighted molecular dynamics simulation of the protein-ligand complex of rhizopuspepsin and inhibitor.
Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
Recombinant rhizopuspepsinogen. Expression, purification, and activation properties of recombinant rhizopuspepsinogens.
Molecular-dynamics investigation of molecular flexibility in ligand binding.
The crystal structure of an acid protease from Rhizopus chinensis at 2.5 A resolution.
Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
Structural study on the active site of porcine pepsin and Rhizopus chinensis acid protease. Spin labeling with diazoketone reagents.
Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.
Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.
Theoretical calculations on the acidity of the active site in aspartic proteinases.
Construction of side-chains in homology modelling. Application to the C-terminal lobe of rhizopuspepsin.
Molecular modeling of the HIV-1 protease and its substrate binding site.
Comparison of inhibitor binding in HIV-1 protease and in non-viral aspartic proteases: the role of the flap.
Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
Structures of complexes of rhizopuspepsin with pepstatin and other statine-containing inhibitors.
Understanding HIV protease: can it be translated into effective therapy against AIDS?
Secondary substrate binding in aspartic proteinases: contributions of subsites S3 and S'2 to kcat.
Application of a self-consistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy.
Relationships of human immunodeficiency virus protease with eukaryotic aspartic proteases.
Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow.
Protein engineering loops in aspartic proteinases: site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin.
Mechanism of action of aspartic proteases.
Purification and crystallization of rhizopuspepsin: the use of nickel chelation chromatography to select for catalytically active species.
Free-energy analysis of enzyme-inhibitor binding: aspartic proteinase-pepstatin complexes.
Design and synthesis of unsymmetrical peptidyl urea inhibitors of aspartic peptidases.
Aspartic protease inhibitors designed from computer-generated templates bind as predicted.
Effect of pH on the structure of rhizopuspepsin.
This enzyme belongs to the peptidase family-A1. According to the literature [5], the catalytic reaction proceeds as follows: (1) Asp218 acts as a general base, abstracting a proton from a water molecule, which is bound between Asp35 and Asp218. (2) The activated water, or the nucleophilic hydroxide ion, makes an attack on the carbonyl carbon atom of the substrate peptide bond, leading to the formation of a tetrahedral transition state with a negatively charged oxyanion (or gem-diol). (3) The protonated carboxyl sidechain of Asp35 stabilzes the negative charge of the transition state. (4) Asp218 acts as a general acid, protonating to the leaving amine group. This step leads to the cleavage of the peptide bond.