LACTATE DEHYDROGENASE : EFFECT OF AMINO ACID CHANGES ON PROPERTIES

Abstract

Many changes have been made by protein engineering in lactate dehydrogenase from B.stearothermophilus. The role of groups involved in susbtrate and coenzyme binding, catalysis and effector molecule binding has been deduced and variants with improved thermal stability developed. The native substrate catalysis patern of lactate dehydrogenase has been modified by many orders of magnitude, to convert this protein into essentially a highly active malate dehydrogenase. Work is Currently on-going to modify this further and to convert malate dehydrogenase, Similarly by protein engineering, into a functional lactate dehydrogenase.