Comparative modelling of barley‐grain aspartic proteinase: A structural rationale for observed hydrolytic specificity

  title={Comparative modelling of barley‐grain aspartic proteinase: A structural rationale for observed hydrolytic specificity},
  author={Kunchur Guruprasad and Kirsi Törmäkangas and Jukka Kervinen and Tom L. Blundell},
  journal={FEBS Letters},
Structure and possible function of aspartic proteinases in barley and other plants.
The aim of this short article is to review the literature on plant aspartic proteinases in general as well as to present more detailed information on our studies on the barley aspartic proteinase.
Structure and function of plant aspartic proteinases.
New questions concerning novel structure-function relationships among plant aspartic proteinases are now starting to be addressed, and their involvement in protein processing or degradation under different conditions and in different stages of plant development suggests some functional specialization.
In Silico Insights into Protein-Protein Interactions and Folding Dynamics of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease
The results indicated that the plant-specific insert may adopt a tertiary structure similar to the characteristic saposin fold and suggest a potential new structural motif among sapos in-fold proteins in the large and diverse SAPLIP family.
Aspartic proteinases: The structures and functions of a versatile superfamily of enzymes
This paper reviews the structure and function of monomeric eukaryotic aspartic proteinases and their inhibitors, including recent analyses of the sequences and the three-dimensional structural models
Construction, expression and characterization of a chimaeric mammalian-plant aspartic proteinase.
This study highlights the use of a chimaeric enzyme strategy in order to characterize unique protein domains within enzyme families, and, for the first time, a putative structure-function role for the PSS as it pertains to plant aspartic proteinases.
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
Structural analysis of prophytepsin led to the identification of a putative membrane receptor‐binding site involved in Golgi‐mediated transport to vacuoles, suggesting that all saposins and saposin‐like domains share a common topology.
Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.*
Based on the crystal structure, a possible mechanism whereby cardosin A might be orientated at the cell surface of the style to interact with its putative receptor from pollen is proposed.
Plant aspartic proteinases: enzymes on the way to a function
Plant aspartic proteinases have been characterized from seeds, flowers and leaves of a number of different species and recent intriguing results suggest possible roles for these enzymes in programmed cell-death of tissues and in pathogen resistance.
Aspartic proteinases in Antarctic fish.


Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D.
Comparison of the N-terminal amino acid sequences of the enzyme subunits with the sequence of the cDNA clone indicates that the heterodimeric enzyme is translated as a proenzyme which is processed into two subunits.
Redesign of the substrate specificity of human cathepsin D: the dominant role of position 287 in the S2 subsite.
It was demonstrated that altering Met287 of human cathepsin D to more polar amino acids produced active mutant enzymes with significantly altered substrate specificity.
Evolution in the structure and function of aspartic proteases
The cDNA structure of rhizopuspepsin suggests the presence of a “pro” enzyme, and it is probable that other fungal aspartic proteases are also synthesized as zymogens.
Knowledge‐based protein modelling and design
A systematic technique for protein modelling that is applicable to the design of drugs, peptide vaccines and novel proteins is described, which simultaneously aligns the known tertiary structures, selects fragments from the structurally conserved regions on the basis of sequence homology, and builds on the loops selected from homologous proteins or a wider database.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC, has been determined by X-ray diffraction at 0.20-nm
A systematic series of synthetic chromophoric substrates for aspartic proteinases.
The Phe-Phe(4-NO2) bond was established as the only peptide bond cleaved, and kinetic constants were obtained for the hydrolysis of these peptide substrates by a representative selection of aspartic proteinases of animal and microbial origin.
Environment‐specific amino acid substitution tables: Tertiary templates and prediction of protein folds
A comparative analysis of families of homologous proteins shows that there are distinct patterns of observed substitutions as a function of local environment, especially for buried polar residues.