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• W2147619645 abstract "Abstract Medium‐chain dehydrogenases/reductases (MDRs) have about 350 to 390 amino acids and belong to a large superfamily of proteins including the Zn‐dependent alcohol dehydrogenases (ADHs) and several other Zn‐dependent activities. They are dimers or tetramers and utilize either NADH or NADPH as electron carriers referred to as cofactors. The oxidation/reduction process is a 2‐electron/1‐proton (hydride ion, H − ) transfer between substrate and cofactor. The compounds oxidized or reduced by these enzymes vary considerably in structure ranging from small primary and secondary alcohols/aldehydes/ketones (aliphatic and aromatic), sugars (sorbitol/fructose, glucose) to large substances like fatty acids, steroids, and retinoids. ADHs are widely distributed in nature and some MDR members are found in all species. An essential Zn ion at the active site is common to all MDRs but some members have two zinc ions per subunit. The 3D Structures of Zn‐dependent MDRs are highly similar and they essentially have the same polypeptide fold. The low sequence identity found sometimes could not immediately reveal this close structural relationship. Now numerous structures have been examined indicating that the evolutionary strategy for MDRs has been to vary amino acids preferably at the reaction center and further away in the substrate binding area. Thus, the size and shape of the substrate channel is adapted for small or large substrates, hydrophilic or hydrophobic substances, modifications attained via few mutations, or significant deletions/additions of amino acids. A further opportunity to create multiplicity has been to vary the control mechanism for the protein conformation change and the oligomeric state. Some enzymes undergo significant structural changes upon cofactor binding, while others do not. A transition state intermediate of NADH in complex with horse liver alcohol dehydrogenase, resolved to atomic resolution (≈1 Å), has revealed structural modifications of the cofactor associated with the activation process for hydride transfer. This involves an OH − pyridine ring adduct, connected to the zinc center. The distortion of the nicotinamide at the enzyme site, affected by the presence of the negatively charged oxygen ligand, influences three parameters: (i) the puckering of the ring, (ii) a deviation from a standard carbon–carbon double bond length, and (iii) accumulation of negative charge at the C4 atom promoting hydride transfer. The active site Zn‐center of this large enzyme group shows great flexibility with respect to metal–ligand geometry and dynamics. Structural and spectroscopic evidence suggest that Zn‐dependent MDRs should be included in the general family of Zn‐enzymes, which require water and hydroxide ion as reactants during catalysis." @default.
• W2147619645 created "2016-06-24" @default.
• W2147619645 creator A5051148950 @default.
• W2147619645 creator A5059029744 @default.
• W2147619645 date "2004-03-05" @default.
• W2147619645 modified "2023-10-03" @default.
• W2147619645 title "<scp>Zn</scp> ‐Dependent Medium‐Chain Dehydrogenases/Reductases" @default.
• W2147619645 cites W1038769719 @default.
• W2147619645 cites W1488493608 @default.
• W2147619645 cites W1494893977 @default.
• W2147619645 cites W1495595158 @default.
• W2147619645 cites W1504516892 @default.
• W2147619645 cites W1510038873 @default.
• W2147619645 cites W1511517285 @default.
• W2147619645 cites W1517249609 @default.
• W2147619645 cites W1539251517 @default.
• W2147619645 cites W1544860800 @default.
• W2147619645 cites W1547353612 @default.
• W2147619645 cites W1548395897 @default.
• W2147619645 cites W1561207830 @default.
• W2147619645 cites W1569170977 @default.
• W2147619645 cites W1578770980 @default.
• W2147619645 cites W1592978800 @default.
• W2147619645 cites W1596588406 @default.
• W2147619645 cites W1626149237 @default.
• W2147619645 cites W1710565104 @default.
• W2147619645 cites W1755321768 @default.
• W2147619645 cites W1757079284 @default.
• W2147619645 cites W1793827344 @default.
• W2147619645 cites W1870988444 @default.
• W2147619645 cites W1886064066 @default.
• W2147619645 cites W1965800528 @default.
• W2147619645 cites W1965991482 @default.
• W2147619645 cites W1971176983 @default.
• W2147619645 cites W1972293382 @default.
• W2147619645 cites W1972475479 @default.
• W2147619645 cites W1972493785 @default.
• W2147619645 cites W1974053931 @default.
• W2147619645 cites W1974284281 @default.
• W2147619645 cites W1975129398 @default.
• W2147619645 cites W1975585381 @default.
• W2147619645 cites W1977384337 @default.
• W2147619645 cites W1977920316 @default.
• W2147619645 cites W1978475663 @default.
• W2147619645 cites W1979066984 @default.
• W2147619645 cites W1979322079 @default.
• W2147619645 cites W1984240812 @default.
• W2147619645 cites W1985485776 @default.
• W2147619645 cites W1985919167 @default.
• W2147619645 cites W1986440320 @default.
• W2147619645 cites W1986743642 @default.
• W2147619645 cites W1986842600 @default.
• W2147619645 cites W1988902379 @default.
• W2147619645 cites W1990057274 @default.
• W2147619645 cites W1990715068 @default.
• W2147619645 cites W1990995914 @default.
• W2147619645 cites W1991140933 @default.
• W2147619645 cites W1991145215 @default.
• W2147619645 cites W1991588154 @default.
• W2147619645 cites W1993702476 @default.
• W2147619645 cites W1999147504 @default.
• W2147619645 cites W2003699602 @default.
• W2147619645 cites W2005539780 @default.
• W2147619645 cites W2005875581 @default.
• W2147619645 cites W2006946214 @default.
• W2147619645 cites W2008428704 @default.
• W2147619645 cites W2008603784 @default.
• W2147619645 cites W2010136126 @default.
• W2147619645 cites W2010162199 @default.
• W2147619645 cites W2010548626 @default.
• W2147619645 cites W2011832476 @default.
• W2147619645 cites W2013921704 @default.
• W2147619645 cites W2014239620 @default.
• W2147619645 cites W2014608237 @default.
• W2147619645 cites W2015171280 @default.
• W2147619645 cites W2016084853 @default.
• W2147619645 cites W2016504665 @default.
• W2147619645 cites W201761757 @default.
• W2147619645 cites W2017774801 @default.
• W2147619645 cites W2018086507 @default.
• W2147619645 cites W2018154356 @default.
• W2147619645 cites W2018809586 @default.
• W2147619645 cites W2018980387 @default.
• W2147619645 cites W2020168271 @default.
• W2147619645 cites W2020940951 @default.
• W2147619645 cites W2020947557 @default.
• W2147619645 cites W2021021514 @default.
• W2147619645 cites W2021723651 @default.
• W2147619645 cites W2022081324 @default.
• W2147619645 cites W2022835362 @default.
• W2147619645 cites W2024953155 @default.
• W2147619645 cites W2024979313 @default.
• W2147619645 cites W2027621854 @default.
• W2147619645 cites W2028162058 @default.
• W2147619645 cites W2028231353 @default.
• W2147619645 cites W2028610299 @default.
• W2147619645 cites W2028712152 @default.
• W2147619645 cites W2029720920 @default.
• W2147619645 cites W2030465353 @default.
• W2147619645 cites W2031636611 @default.

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