کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048879 | 1074104 | 2010 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases](/preview/png/2048879.png)
2,3-Butanediol dehydrogenase (BDH) catalyzes the NAD-dependent redox reaction between acetoin and 2,3-butanediol. There are three types of homologous BDH, each stereospecific for both substrate and product. To establish how these homologous enzymes possess differential stereospecificities, we determined the crystal structure of l-BDH with a bound inhibitor at 2.0 Å. Comparison with the inhibitor binding mode of meso-BDH highlights the role of a hydrogen-bond from a conserved Trp residue192. Site-directed mutagenesis of three active site residues of meso-BDH, including Trp190, which corresponds to Trp192 of l-BDH, converted its stereospecificity to that of l-BDH. This result confirms the importance of conserved residues in modifying the stereospecificity of homologous enzymes.
Journal: FEBS Letters - Volume 584, Issue 1, 4 January 2010, Pages 219–223