Honors Program


Date of this Version

Fall 11-1-2019

Document Type



Kester, K. 2019. Effect of a Site-Directed Mutagenesis at the NAD/NADH Binding Site on Malate Dehydrogenase Activity. Undergraduate Honors Thesis. University of Nebraska-Lincoln.


Copyright Kayla Kester 2019.


Malate Dehydrogenase (MDH) is an enzyme found in many organisms that catalyzes the reversible oxidation-reduction reaction of malate to oxaloacetate through the transfer of a hydride ion. A nucleotide cofactor, nicotinamide adenine dinucleotide (NAD) is required for the catalysis. MDH is a key enzyme in various cellular activities and exists in several forms in locations including the cytoplasm, mitochondria, and glyoxysome. While much is known about the structure and related function of malate dehydrogenase and cofactor, NAD, there is more to be discovered about the role of specific amino acid residues at the highly conserved amino acid sequence of the NAD binding site on malate dehydrogenase activity.