Enzyme design with remote effects
Chemists in M?im devise a new way of optimizing enzymes for industrial applicationsEngineers are unlikely to tinker with the cooling system if they want to increase the size of an engine. Yet chemists at the Max Planck Institute for Coal Research have adopted an approach similar to this in their efforts to optimize an enzyme for practical applications. They substituted two amino acids at a site relatively distal to the biocatalyst?s binding pocket, the location where the chemical reaction takes place. This modification alters the overall structure of the enzyme in such a way that it can now convert a larger number of different chemical compounds. In addition, it produces preferentially one of two possible enantiomers which arise as what is known as a racemic mixture during traditional synthesis. Although they are chemically identical, the enantiomers differ in terms of their structure, like a right and left hand. Only one of the two versions is usually suitable for use as a medically active agent. Thanks t
Enzyme design with remote effects
Engineers are unlikely to tinker with the cooling system if they want to increase the size of an engine. Yet chemists at the Max Planck Institute for Coal Research have adopted an approach similar ...
Tue 16 Feb 10 from PhysOrg
Enzyme design with remote effects: Chemists devise new way of optimizing enzymes for industrial applications, Tue 16 Feb 10 from ScienceDaily
Enzyme Design With Remote Effects, Tue 16 Feb 10 from RedOrbit
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