Reference - Detail
| RRC ID | 55159 |
|---|---|
| Author | Wang B, Ji SQ, Ma XQ, Lu M, Wang LS, Li FL. |
| Title | Substitution of one calcium-binding amino acid strengthens substrate binding in a thermophilic alginate lyase. |
| Journal | FEBS Lett |
| Abstract |
Ligand binding is sensitive to temperatures since noncovalent bonds between the binding site and ligand could be broken by heat. How metal ion-binding amino acids in alginate lyase evolve to achieve tight substrate binding in a hostile environment remains unknown. An endolytic alginate lyase AlgAT0 specifically cleaved the M-G glycosidic bond and released disaccharides as the main end product. Four conserved calcium-binding sites were predicted and the supplement of Ca2+ led to enhanced substrate binding and protein stability. Among the four conserved calcium-binding sites, one substitution of aspartate for glutamate in AlgAT0 was proved to stimulate Ca2+ affinity. This study suggested that substrate affinity of polysaccharide lyases could be improved by tight binding to Ca2+ via one amino acid substitution. |
| Volume | 592(3) |
| Pages | 369-379 |
| Published | 2018-2-1 |
| DOI | 10.1002/1873-3468.12965 |
| PMID | 29292503 |
| MeSH | Amino Acid Substitution* Binding Sites Calcium / metabolism* Calorimetry, Differential Scanning Circular Dichroism Disaccharides / metabolism Models, Molecular Polysaccharide-Lyases / chemistry* Polysaccharide-Lyases / genetics Polysaccharide-Lyases / metabolism* Protein Conformation Substrate Specificity Thermodynamics |
| IF | 2.675 |
| Times Cited | 2 |
| Resource | |
| General Microbes | JCM 30481 |