Involvement of glycine and aspartate residues in the binding capacity of FAD in the NADH dehydrogenase from an alkaliphilic Bacillus |
| |
Authors: | Shiraki Masato Koyama Noriyuki |
| |
Institution: | Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan. |
| |
Abstract: | There is a region exhibiting a similarity of amino acid sequence near the carboxyl-terminal segment of each FAD-containing oxidoreductase. In this region, four amino acid residues-Thr, Ala, Gly, and Asp-are highly conserved. To determine the involvement of the four amino acid residues (Thr-469, Ala-476, Gly-478, and Asp-479) in the activity of NADH dehydrogenase of an alkaliphilic Bacillus, mutations of these amino acid residues were conducted. In spite of high conservation, mutations of Thr-469 and Ala-476 to Ala and Ser, respectively, did not lead to a critical loss of enzyme activity. However, mutations of Gly-478 and Asp-479 to Ala caused a complete loss of the activity, which appears to result from the loss of binding capacity of FAD. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|