| Autor: |
ZAMEER, M., RAFIQUE, A., ALYAS, S., FARRUKH, S. Y., TAHIR, U., ZAHRA, N., ALI, Q., KHAN, M. T., MAZHAR, M., RUKHSAR, A., QURESHI, J. A., SHABBIR, A., SATTAR, H., SOHAIL, A. |
| Předmět: |
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| Zdroj: |
Applied Ecology & Environmental Research; 2023, Vol. 21 Issue 2, p925-941, 17p |
| Abstrakt: |
Climate change, dramatic fluctuations in the cost of fuel can cause an increase in the prices of basic food items. Pakistan is undergoing a serious energy crisis. Fortunately, this degrading situation is countered with the help of biomass energy (bioethanol) invention. However, the selection of the best strains with efficient enzymes for the production of bioethanol is in a continuous process of improvement. The objective of this work is to compare and analyze the structure of extremophilic strains with currently used organisms. Protein sequences of two different strains both zinc- and iron-dependent alcohol dehydrogenases (ADHs) were retrieved from Uniprot. Sequence analysis using protein sequence was conducted separately for both Zn- and Fe strains with Saccharomycescervisae and Zymomonasmobilis respectively with the help of T-coffee and Aliview. 3D protein structure modelswere built using the swiss model. The accuracy of predicted models was confirmed through online servers molprobity, ERRAT score VERIFY 3D values, and VADAR. Upon acquiring complete structural information of target strains, mutations were carried out in Fe and Zn-based organisms to check the best conformation of the enzyme for maximum bioethanol yield. The study demonstrated that the ability to withstand high-temperature ADH of thermophilic bacteria is considered a key enzyme for bioethanol production. Metal-binding residue sites His-62, Cys-38, Glu-63, and Cys-154 in Zn strains and Asp-204, His-208, His-271, and His-285 in Fe strains was conserved. Ligand interaction with residues in Fe and Zn strains was found similar in Saccharomycescervisae and Zymomonasmobilis strains. Structural and mutational analyses were performed to interpret the significance of mutated residues (A62, A38, Q63, A154 in Sulfolobus acidoculdarius and E204, R208, R271, R285 in Archaeglobus fulgidus) at the active binding site of ADH. Mutations at the active binding site in both Fe and Zn dependent ADH will impair structural stability, disturbance in catalytic pockets and bonds hence subordinating the overall enzyme-substrate complex and decreased efficiency in binding lignocellulosic biomass as substrate. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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