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Title: Lactate dehydrogenase displays absolute stereospecificity in the transfer of the prochiral hydrogen of NADH. Author: LaReau RD, Anderson VE. Journal: J Biol Chem; 1989 Sep 15; 264(26):15338-43. PubMed ID: 2670938. Abstract: The frequency of nonstereospecific hydride transfers to and from the C-4 of NAD+ by porcine heart lactate dehydrogenase has been determined to be less than 1 out of every 10(7) hydride transfers, using a method employing a dynamic equilibrium which allows for the detection of extremely rare (less than 1 in 10(8] nonstereospecific transfers. A detailed protocol is presented. The inability to detect unequivocally a nonstereospecific transfer either to or from the si face of the nicotinamide ring (pro-4S hydrogen to NADH) indicates that the transition state for the more favorable transfer of the pro-4R hydrogen is at least 10 kcal/mol lower in energy.[Abstract] [Full Text] [Related] [New Search]