35 by: Clay Roper-Daniels
Student – Clay Roper-Daniels
Name of Enzyme & E.C Number – Glycerol dehydrogenase (GlyDH), E.C. #1.1.1.6
Where is enzyme found? Glycerol dehydrogenase has been discovered in many organisms, which include bacteria, fungi, yeast, and mammals. However, the organism that has been most utilized to study GlyDH has been the bacteria Klebsiella pneumoniae. The reason for this is that Klebsiella pneumoniae possesses two genes (dhaD and gldA) encoding GlyDH, both of which are complementary to each other from gene duplication (Soo Ko et al., 2024).
What does the enzyme do? In microorganisms, glycerol is used as a carbon and energy source during fermentation. Glycerol dehydrogenase initiates the first step of the glycerol metabolism pathway by converting glycerol into dihydroxyacetone (Soo Ko et al., 2020). This reaction relies on NAD+ in the active site as an electron-accepting cofactor. Additionally, a monovalent cation is necessary for catalytic activity and the positioning of the glycerol substrate (Leichus & Blanchard, 1994). Also, GlyDH has a broad specificity to other substrates, making it versatile in biochemical processes.
Any other interesting facts or important information on your enzyme – Glycerol dehydrogenase has many applications in the biofuel industry. In the production of biodiesel, the generation of glycerol accounts for 10% of all byproducts (Kumar et al., 2015). As a result, new research has been inspired to find effective ways of utilizing glycerol products. The most promising product being dihydroxyacetone, as it has a high value in the cosmetic market.
References:
Ko, G. S., Nguyen, Q. T., Kim, D. H. & Yang, J. K. (2020). Biochemical and Molecular Characterization of Glycerol Dehydrogenase from Klebsiella pneumoniae. Journal of Microbiology and Biotechnology, 30(2), 271–278. https://doi.org/10.4014/jmb.1909.09056
Ko, G. S., Nguyen, Q. T., Koh, S. & Kang, W. (2024). Crystal Structure of Glycerol Dehydrogenase from Klebsiella pneumoniae. Journal of the Korean Chemical Society, 68(1), 32-39. https://doi.org/10.5012/jkcs.2024.68.1.32
Kumar, G. S., Wee, Y., Lee, I., Sun, H. J., Zhao, X., Xia, S., Kim, S., Lee, J., Wang, P. & Kim, J. (2015). Stabilized glycerol dehydrogenase for the conversion of glycerol to dihydroxyacetone. Chemical Engineering Journal, 276, 283–288. https://doi.org/10.1016/j.cej.2015.04.039
Leichus, B. N., & Blanchard, J. S. (1994). Isotopic Analysis of the Reaction Catalyzed by Glycerol Dehydrogenase. Biochemistry, 33(48), 14642–14649. https://doi.org/10.1021/bi00252a033
Velasco-Lozano, S., Roca, M., Leal-Duaso, A., Mayoral, J. A., Pires, E., Moliner, V., & López-Gallego, F. (2020). Selective oxidation of alkyl and aryl glyceryl monoethers catalysed by an engineered and immobilized glycerol dehydrogenase. Chemical Science, 11(44), 12009–12020. https://doi.org/10.1039/d0sc04471g
Zhang, J., Nanjaraj Urs, A. N., Lin, L., Zhou, Y., Hu, Y., Hua, G., Gao, Q., Yuchi, Z., & Zhang, Y. (2019). Structure of glycerol dehydrogenase (GldA) from Escherichia coli. Acta Crystallographica Section F Structural Biology Communications, 75(3), 176–183. https://doi.org/10.1107/s2053230x19000037
