Directory of Therapeutic Enzymes by Barry M. McGrath, Gary Walsh

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By Barry M. McGrath, Gary Walsh

Conscientiously crafted to supply tightly targeted and authoritative details, the Directory of healing Enzymes covers all authorized healing enzymes presently utilized in drugs. Written usually via specialists, the booklet comprises info sourced without delay from the corporate that constructed or synthetic the product. It explores significant improvement concerns, from production and advertising to supply of the completed product.

Chapter 1 experiences utilized enzymology whereas bankruptcy 2 delineates thought and purposes. among them, the 1st chapters set the perfect backdrop for the remainder chapters, which specialize in genuine enzyme items that experience received regulatory popularity of common scientific use. The bankruptcy authors talk about the biochemistry of the enzymes, the reactions they catalyze, how they're produced or synthetic, and their scientific purposes.

The ebook highlights the various purposes of authorized healing enzymes, together with use within the therapy of blood-clotting issues, sure cancers, and numerous genetic issues. Illustrated with tables and figures that aid the textual content, the publication is a unmarried resource of in-depth technical information.

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Currently, furanone is produced synthetically from expensive 2,5-hex-3-ynediol. Newman et al. [189] report the use of directed evolution to enable the enzymatic synthesis of furanone from the relatively inexpensive p-xylene. A bacterial toluene dioxygenase operon was subjected to DNA shuffling to improve the biotransformation of a range of aromatic compounds. An increase in the substrate specificity and selectivity of the toluene dioxygenase system was achieved, such that an alternative, commercially viable, enzyme-driven preparation of furanone is now available [189].

Site-specific recombinases have recently been applied to experimental biology, biotechnology, and gene therapy. Several recent reports describe the directed evolution of prokaryotic recombinases to insert into mammalian cells [185–187], with applications as tools for modifying the genomes of eukaryotic cells [188]. For example, Sclimenti et al. [186] report the evolution of phage ΦC31 integrase to target a specific DNA sequence in the human genome. The wild-type phage integrase recombines sequences in a semirandom fashion in the human genome.

183] report applying directed evolution to evolve a DNA polymerase into an efficient RNA polymerase. Restriction enzymes are an indispensable tool for molecular biologists. The ability to engineer restriction endonucleases with altered recognition sequences is needed for biotechnology and medical applications [180]. The substrate range of the promiscuous restriction endonuclease BstYI was narrowed using directed evolution. The variant endonuclease displayed a 12-fold increase in DNA sequence specificity [184].

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