Structural highlights
Publication Abstract from PubMed
alpha-l-Rhamnosidases are catalysts of industrial tremendous interest, but their uses are still somewhat limited by their poor thermal stabilities and selectivities. The thermophilic DtRha from Dictyoglomus thermophilum 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 alpha-l-rhamnose. Most significantly, DtRha demonstrated to have a stronger preference for alpha(1 --> 2) linkage rather than alpha(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.
Biochemical Characterization of the alpha-l-Rhamnosidase DtRha from Dictyoglomus thermophilum: Application to the Selective Derhamnosylation of Natural Flavonoids.,Guillotin L, Kim H, Traore Y, Moreau P, Lafite P, Coquoin V, Nuccio S, de Vaumas R, Daniellou R ACS Omega. 2019 Jan 24;4(1):1916-1922. doi: 10.1021/acsomega.8b03186. eCollection, 2019 Jan 31. PMID:31459445[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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-Rhamnosidase DtRha from Dictyoglomus thermophilum: Application to the Selective Derhamnosylation of Natural Flavonoids. ACS Omega. 2019 Jan 24;4(1):1916-1922. doi: 10.1021/acsomega.8b03186. eCollection, 2019 Jan 31. PMID:31459445 doi:http://dx.doi.org/10.1021/acsomega.8b03186
