Chemical modification of biocatalysts.
Although several powerful methods exist for the redesign of enzyme structure and function these are typically limited to the 20 most abundant proteinogenic amino acids. The use of chemical modification overcomes this limitation to allow virtually unlimited alteration of amino acid sidechain structures. If heterogeneous mixtures of enzyme products are to be avoided, however, the required chemistry should be efficient, selective and compatible with aqueous conditions. Recent advances have been made in the modification of proteinases, aminotransferases and redox enzymes.
Davis
Benjamin G
BG
Dyson Perrins Laboratory, Department of Chemistry, South Parks Road, Oxford OX1 3QY, UK. ben.davis@chemistry.oxford.ac.uk
D010450:Endopeptidases / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry*; D005949:Glucose Oxidase / Q000737:chemistry; D005979:Glutathione Peroxidase / Q000737:chemistry; D007553:Isotope Labeling; D008049:Lipase / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D015202:Protein Engineering / Q000379:methods*; D012260:Ribonucleases / Q000737:chemistry
D004798:Enzymes; D005949:Glucose Oxidase; D005979:Glutathione Peroxidase; D012260:Ribonucleases; D008049:Lipase; D010450:Endopeptidases