By Herbert A Kirst, Wu-Kuang Yeh
Eli Lily and corporate, Greenfield, identity. Reference offering an up to date overview of enzyme capabilities in human and animal overall healthiness, together with assurance of latest and rising applied sciences in biotechnical and pharmaceutical industries. Emphasizes sleek tools of metabolic engineering and drug discovery tactics, and info enzymes with regards to human ailment.
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Additional resources for Enzyme Technologies for Pharmaceutical and Biotechnological Applications
Current engineering approaches which have been performed include the following alterations of domain positions. 1. 2. 3. The replacement of product amino acid residues by positional alteration of domains [102,103]. The cysteine- and valine-specific activation-thiolation didomains of P. chrysogenum ACV synthetase have been successfully inserted into the terminal position of surfactin synthetase in Bacillus subtilis . , specific domains could be replaced to generate new tripeptides or to improve the efficiency of poorly incorporated amino acid analogues.
Mol Gen Genet 57:308–318, 1998. F de Ferra, F Rodriguez, O Tortora, C Tosi, G Grandi. Engineering of peptide synthetases. Key role of the thioesterase-like domain for efficient production of recombinant peptides. J Biol Chem 272:25304–25309, 1997. E Guenzi, G Galli, I Grgurina, E Pace, P Ferranti, G Grandi. Coordinate transcription and physical linkage of domains in surfactin synthetase are not essential for proper assembly and activity of the multienzyme complex. J Biol Chem 273: 14403–14410, 1998.
A. a. ϩ von Do¨hren et al. 16 Table 4 Continued Substrate 2R,3S-2-Amino-3-fluoro-butyrate 2R,3R-2-Amino-3-fluoro-butyrate L-Phe L-Tyr L-Trp L-His L-Pro L-Met 3-Ala 4-Abu ACVS A. chrysogenuma ACVS S. a. a. ϩϩϩϩ ϩϩ ϩ ϩϩ ϩ Ϫ ϩ (ϩ) Activities are given by: Ϫ, not detected or significant (Ͻ1%); (ϩ), 1–5%; ϩ, 5–10%; ϩϩ, 10– 50%; ϩϩϩ, 50–100%; ϩϩϩϩ, 100% or Ͼ100% relative to natural main substrate. b Data have been taken mainly from Ref. 51. c Note that there are large differences in the rates of Aad activation between the fungal and bacterial enzymes.