N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH.
An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.
Disulfide bonds of pepsinogen and pepsin: identification of the disulfide bonds which can be reversibly reduced and reoxidized.
The pepsin catalysed hydrolysis of bis-P-nitrophenyl sulfite.
Evidence for an acyl intermediate in pepsin-catalysed reactions.
Acyl and amino intermediates in reactions catalysed by pig pepsin. Analysis of transpeptidation products.
X-ray crystallographic studies of pepsin.
Mechanism of pepsin catalysis: general base catalysis by the active-site carboxylate ion.
The effect of polycations on the activity of pepsin.
The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2.
Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.
A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanism.
X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
Why does pepsin have a negative charge at very low pH? An analysis of conserved charged residues in aspartic proteinases.
The number of cooperative regions (energetic domains) in a pepsin molecule depends on the pH of the medium.
Pepsin-catalyzed peptide synthesis in biphasic systems.
Pepsin behavior as a catalyst in equilibrium-controlled peptide synthesis.
Refined structure of porcine pepsinogen at 1.8 A resolution.
Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor.
Pepsin as a catalyst of peptide synthesis. Enzyme co-precipitation with emerging peptide products.
Enzymic activities of two-chain pepsinogen, two-chain pepsin, and the amino-terminal lobe of pepsinogen.
pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
The high-resolution crystal structure of porcine pepsinogen.
A quantum mechanical study of the active site of aspartic proteinases.
Conformational instability of the N- and C-terminal lobes of porcine pepsin in neutral and alkaline solutions.
Aspartic proteinases--Fourier transform IR studies of the aspartic carboxylic groups in the active site of pepsin.
Mechanism of pepsin-catalyzed aminotranspeptidation reactions.
Pepsin-catalyzed peptide synthesis in organic media: studies with free and immobilized enzyme.
A new way of looking at aspartic proteinase structures: a comparison of pepsin structure to other aspartic proteinases in the near active site region.
Evidence for electrostatic interactions in the S2 subsite of porcine pepsin.
Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates.
The sole lysine residue in porcine pepsin works as a key residue for catalysis and conformational flexibility.
Restrained molecular dynamics study of the interaction between bovine kappa-casein peptide 98-111 and bovine chymosin and porcine pepsin.
Crystal structure of human pepsin and its complex with pepstatin.
Proteinase-catalyzed peptide synthesis in concentrated solutions of urea and other denaturing agents.
Engineering of porcine pepsin. Alteration of S1 substrate specificity of pepsin to those of fungal aspartic proteinases by site-directed mutagenesis.
Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua).
Pepsin as a catalyst for peptide synthesis: formation of peptide bonds not typical for pepsin substrate specificity.
The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A.
Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog.
The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.
Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.
Structure of human uropepsin at 2.45 A resolution.
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
A history of pepsin and related enzymes.
This enzyme belongs to the peptidase family-A1. This enzyme is closely related to the counter part enzyme (D00436 in EzCatDB). According to the literature [10], [25] & [41], the catalytic reaction proceeds as follows: (1) Asp215 acts as a general base, abstracting a proton from a water molecule, which is bound between Asp32 and Asp215. (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 Asp32 stabilzes the negative charge of the transition state. (4) Asp215 acts as a general acid, protonating to the leaving amine group. This step leads to the cleavage of the peptide bond.