De Novo Design of Catalysts,Antibodies or Abzymes,Molecules,Peptide Biocatalysts,Enzymes,BiologicalRibozymes,Re Engineered Enzymes

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Protein and Enzymes Engineering Protein and Enzymes Engineering - Introduction Engineering of Macromolecules Basic Outline Protein Engineering vs Enzyme Engineering for a Biocatalyst Protein Engineering Rationale of Protein Enzyme Engineering Basic Assumptions for Protein Engineering Key Biocatalyst Properties that are Altered Through Protein Engineering Some Examples of Improved Kinetic Parameters of Enzymes Turnover Determined by k_cat Selectivity and Specificity Some Technologies Available for Enchancing Biocatalyst Characteristics Molecular Stability Catalytic Diversity Acquiring Knowledge for Protein Engineering Study of Protein Structure Three Dimensional Protein Modeling Perturbation Theory

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De novo Design of Catalysts
Sometimes existing enzymes provide no solutions for the intended reactions. In such cases molecules evolved for purposes other than catalysis may be engineered to function as enzymes. Antibodies or enzymes provide one such example, although they have low expression, limited stability and low turnover rates, thus making their commercial exploitation difficult. These enzymes, however, were generated in response to molecules that mimic the transition state of a reaction. Molecules other than antibodies can also be used for this purpose.

Peptide biocatalysts (de novo designed) failed as enzymes.
Natural biocatalysts of enzymes sometimes pose serious problems, Sometimes, enzymes are too unwieldy, or the because, either the biological pathways are too combersome. Alternatives, therefore, have been sought and following types of novel biocatalysts have been generated and tried: (i) enzymes (catalytic antibodies); (ii) re-engineered enzymes (RNES); (iii) ribozymes (catalytic RNA); (iv) de novo design (peptides, etc.).
Among these, the first three approaches have shown some promise, although so far none of these could be put to industrial use. However, two efforts for the synthesis of peptides (CHZ-1, Ch_z P_epz and T_rP_epz) to be used as chymotrypsin and trypsin, reported in early 1990s, could not be repeated later.
Therefore, the initial hope of the future of peptides as enzymes was not fulfilifed, and the small peptides representing mere catalytic sites, no longer provide an exciting alternative for biocatalysts. Only in future, we will know if enzymes and ribozymes, could be suitable alternatives, although RNAs certainly have a promise.

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Methods for Protein Engineering Site Directed Mutagenesis in Vivo Gene Modification Through Oligonucleotide Synthesis Breeding a Better Catalyst Using Random Events Artificial Random Mutagenesis Random DNA Shuffing Using Recombination Combination of Structure Based and Envolutionary Approaches Multienzyme Systems bi and Polyfunctional Enzymes by Gene Fusion Chemical Modification of Enzymes Production of Site Specific Nucleases Production of Artifical Semi Synthetic Oxido Reductases Flavo Enzyme Hybrid Enzymes Combinatorial Chemistry Organic Synthesis Libraries De Novo Design of Catalysts Some Early Achievements of Protein Engineering Possible Candidates for Future Protein Engineering Improving Enzymes by Using Organic Solvents