Fulco, Umberto LainoSouza, Lucas Marques de2021-03-052021-03-052020-10-30SOUZA, Lucas Marques de. Análise quântica das interações entre a enzima AKR1D1 com os hormônios esteroides testosterona e progesterona. 2020. 62f. Dissertação (Mestrado em Ciências Biológicas) - Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, 2020.https://repositorio.ufrn.br/handle/123456789/31726The enzyme Δ4-3-cetosteroid 5β-Human Redutase (AKR1D1) is an essential regulator for bioavailability of steroids and metabolic phenotype. Its activity is directly related to diseases such as: obesity, type 2 diabetes mellitus, nonalcoholic fatty liver disease, among others. Understanding how this enzyme works is of great importance to improve speed and efficiency in the development of disease treatments. Bearing this in mind, interactions between enzyme AKR1D1 with the two main masculine and feminine steroid hormones, testosterone and progesterone respectively, have been analyzed using quantum mechanics and computational simulation techniques - the density-functional theory (DFT) and the molecular fractionation with conjugate caps (MFCC) method. In the complex Testosterone-AKR1D1 the amino acid residues that mostly contributed to attraction were: TRP230 > TYR26 > ASN227 > TYR132 > SER225; in complex Progesterone-AKR1D1 they were: GLU120 > TRP230 > TYR58 > TYR132 > ILE57. The complex with Testosterone, located in the allosteric site of the protein, presented a higher energy of total interaction when compared to the location of progesterone in the active site. The residue TRP230 had a prominent role in both systems, reinforcing its important function of positioning the binder inside the enzyme. And GLU120, residue of the catalytic tetrad, showed the highest energy of interaction of AKR1D1 with progesterone.Acesso AbertoAKR1D1Hormônios esteroidesTestosteronaProgesteronaDFTMFCCmasterThesis