Penicillium janthinellum aspartic proteinase
Penicillium janthinellum acid proteinase
Penicillium expansum aspartic proteinase
Penicillium caseicolum aspartic proteinase
Penicillium citrinum aspartic proteinase
Amino acid sequence around the active site aspartic acid in penicillopepsin.
An X-ray crystallographic approach to enzyme structure and function.
Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.
Structure and refinement of penicillopepsin at 1.8 A resolution.
X-ray crystallography (ISBN: 0935940022)
Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium
Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution.
Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions.
Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin.
Inhibition of aspartic proteases by pepstatin and 3-methylstatine derivatives of pepstatin. Evidence for collected-substrate enzyme inhibition.
Molecular dynamics study of the structure and dynamics of a protein molecule in a crystalline ionic environment, Streptomyces griseus protease A.
X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
Modeling of globular proteins. A distance-based data search procedure for the construction of insertion/deletion regions and Pro----non-Pro mutations.
Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
Studies on the mechanism of action of penicillopepsin.
Mechanism and pathway of penicillopepsin-catalyzed transpeptidation and evidence for noncovalent trapping of amino acid and peptide intermediates.
Refined structure of porcine pepsinogen at 1.8 A resolution.
Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues.
Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
Crystallization and preliminary crystallographic characterization of aspartic proteinase-A from baker's yeast and its complexes with inhibitors.
Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.
Critical-point analysis in protein electron-density map interpretation.
Overcoming the unfavourable entropic contribution of ligand binding with a macrocyclic inhibitor bound to penicillopepsin.
Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes.
Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).
Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water.
This enzyme belongs to the peptidase family-A1. This enzyme has got a catalytic dyad, composed of two aspartic acid residues, which is observed in other aspartate proteases, such as pepsin (D00436 in EzCatDB). It suggests that it may have a similar reaction mechanism.