Alteration of enzyme specificity and catalysis by protein engineering.
New substrate specificities can be introduced into existing enzymes for the purpose of making them more suitable for the chemoenzymic synthesis of single compound drugs and other chiral compounds. The most productive route used in the past year has involved the utilization of the catalytic and substrate-binding properties from homologous enzymes found in nature, one example being the broadening of the substrate specificity of yeast alcohol dehydrogenase. Other highlights include the creation of thermostable dehydrogenases that will interconvert NADPH and NADH, and the design of mutant enzymes with improved catalytic rates compared with their wild-type counterparts.
Molecular Recognition Centre, School of Medical Sciences, University of Bristol, UK.
H M
HM
Wilks
J J
JJ
Holbrook
D000595:Amino Acid Sequence; D002384:Catalysis; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015202:Protein Engineering; D013379:Substrate Specificity
D004798:Enzymes