6I60

Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum

6I60 の概要

• エントリーDOI: 10.2210/pdb6i60/pdb
• 分子名称: Alpha-rhamnosidase, TRIETHYLENE GLYCOL, 2-(2-ETHOXYETHOXY)ETHANOL, ... (4 entities in total)
• 機能のキーワード: glycoside hydrolase, substrate, hydrolase
• 由来する生物種: Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 221464.38

構造登録者

Lafite, P.,Daniellou, R. (登録日: 2018-11-15, 公開日: 2019-02-06, 最終更新日: 2024-01-24)

主引用文献

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

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: 31459445
DOI: 10.1021/acsomega.8b03186

実験手法

X-RAY DIFFRACTION (2.743 Å)