6I60
Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum
Summary for 6I60
| Entry DOI | 10.2210/pdb6i60/pdb |
| Descriptor | Alpha-rhamnosidase, TRIETHYLENE GLYCOL, 2-(2-ETHOXYETHOXY)ETHANOL, ... (4 entities in total) |
| Functional Keywords | glycoside hydrolase, substrate, hydrolase |
| Biological source | Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) |
| Total number of polymer chains | 2 |
| Total formula weight | 221464.38 |
| Authors | Lafite, P.,Daniellou, R. (deposition date: 2018-11-15, release date: 2019-02-06, Last modification date: 2024-01-24) |
| Primary citation | Guillotin, L.,Kim, H.,Traore, Y.,Moreau, P.,Lafite, P.,Coquoin, V.,Nuccio, S.,de Vaumas, R.,Daniellou, R. Biochemical Characterization of the alpha-l-RhamnosidaseDtRha fromDictyoglomus thermophilum: Application to the Selective Derhamnosylation of Natural Flavonoids. Acs Omega, 4:1916-1922, 2019 Cited by PubMed Abstract: α-l-Rhamnosidases are catalysts of industrial tremendous interest, but their uses are still somewhat limited by their poor thermal stabilities and selectivities. The thermophilic Rha from was cloned, and the recombinant protein was easily purified to homogeneity to afford 4.5 mg/L culture of biocatalyst. Michaelis-Menten parameters demonstrated it to be fully specific for α-l-rhamnose. Most significantly, Rha demonstrated to have a stronger preference for α(1 → 2) linkage rather than α(1 → 6) linkage when removing rhamnosyl moiety from natural flavonoids. This selectivity was fully explained by the difference of binding of the corresponding substrates in the active site of the protein. PubMed: 31459445DOI: 10.1021/acsomega.8b03186 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.743 Å) |
Structure validation
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