46 by: Ashton Ashley
Student: Ashton Ashley
Enzyme: Maleate Isomerase
E.C. Number: 5.2.1.1
Where is Maleate Isomerase found? The enzyme maleate isomerase is typically found in multiple bacteria species. The particular one mentioned in my enzyme tale is Nocardia farcinica, which can be found in soils and dust throughout the world.
What does the enzyme do? Maleate isomerase is largely responsible for the cis-trans isomerization of maleate to fumarate. In other words, it breaks a carbon – carbon bond (C2 – C3) in order to rotate it from cis to trans orientation, then re-establish the carbon – carbon double bond. It performs this process with assistance from Cysteine76 and Cysteine194, particularly the thiol protons (those attached to sulfur). This enzyme participates in various metabolic processes, such as that of nicotinate and butanoate. It is particularly needed for the final step in the breakdown of nicotinic acid, which the process outlined in my enzyme tale.
Any other interesting facts or important info? Maleate isomerase is actually unstable, even at moderate temperatures! Given this, heat stable maleate isomerases have been engineered and applied. On such application, is the industrial degradation of tobacco waste.
References
Fisch, F., Fleites, C. M., Delenne, M., Baudendistel, N., Hauer, B., Turkenburg, J. P., Hart, S., Bruce, N. C., & Grogan, G. (2010). A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase. Journal of the American Chemical Society, 132(33), 11455–11457. https://doi.org/10.1021/ja1053576
Roa Engel, C. A., Straathof, A. J. J., Zijlmans, T. W., van Gulik, W. M., & van der Wielen, L. A. M. (2008, March). Fumaric acid production by fermentation. Applied microbiology and biotechnology. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2243254
Tang, H., Yao, Y., Wang, L., Yu, H., Ren, Y., Wu, G., & Xu, P. (2012a). Genomic analysis of pseudomonas putida: Genes in a genome island are crucial for nicotine degradation. Scientific Reports, 2(1). https://doi.org/10.1038/srep00377
