The D-Lactate Dehydrogenase from Sporolactobacillus inulinus Also Possessing Reversible Deamination ActivityReport as inadecuate




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Hydroxyacid dehydrogenases are responsible for the conversion of 2-keto acids to 2-hydroxyacids and have a wide range of biotechnological applications. In this study, a D-lactate dehydrogenase D-LDH from a Sporolactobacillus inulinus strain was experimentally verified to have both the D-LDH and glutamate dehydrogenase GDH activities reversible deamination. The catalytic mechanism was demonstrated by identification of key residues from the crystal structure analysis and site-directed mutagenesis. The Arg234 and Gly79 residues of this enzyme play a significant role in both D-LDH and GDH activities. His295 and Phe298 in DLDH744 were identified to be key residues for lactate dehydrogenase LDH activity only whereas Tyr101 is a unique residue that is critical for GDH activity. Characterization of the biochemical properties contributes to understanding of the catalytic mechanism of this novel D-lactate dehydrogenase enzyme.



Author: Lingfeng Zhu, Xiaoling Xu, Limin Wang, Hui Dong , Bo Yu

Source: http://plos.srce.hr/



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