MitoNEET is a [2Fe-2S]-cluster containing protein located in the outer mitochondrial membrane that has been investigated as a potential drug development for Type 2 diabetes, Parkinson’s disease, and cancer. MitoNEET is a homodimer with each monomer containing 3 cysteine and 1 histidine ligation residues, where this area contains a hydrogen-bonding network with His87 and lys55. Our hypothesis is that this site is an enzyme active site at which mitoNEET functions as a transaminase enzyme. The known binding interaction between L-Cysteine and mitoNEET-PLP from past investigations will allow us to determine that 3-Mercaptopyruvate and Glutamate are the products of the transaminase reaction. With the help of Lactate Dehydrogenase, an enzyme that catalyzes the reaction of lactate to pyruvate, utilizing NAD+ to NADH by reducing lactate. This known reaction allows us to determine the presence of 3-Mercaptopyruvate via oxidation of NADH to NAD+ to form 3-mercaptolactate via the UV-Vis Spectrometer analysis at 340 nm wavelength. We found a decreasing absorbance of NADH, indicating that the presence of 3-Mercaptopyruvate is present in the solution, proving that transamination reaction occurred. This finding provides more understanding of mitoNEET enzymology, which further helps find more effective development of drugs.

Characterizing MitoNEET as a transaminase enzyme via analysis of 3-mercaptopyruvate

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