6S9V

Crystal structure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum

6S9V の概要

• エントリーDOI: 10.2210/pdb6s9v/pdb
• 分子名称: Sucrose 6(F)-phosphate phosphorylase, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: glycoside phosphorylase, sucrose 6-phosphate, glycoside hydrolase family gh13-18, transferase
• 由来する生物種: Thermoanaerobacterium thermosaccharolyticum DSM 571
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 118730.75

構造登録者

Capra, N.,Franceus, J.,Desmet, T.,Thunnissen, A.M.W.H. (登録日: 2019-07-15, 公開日: 2019-08-28, 最終更新日: 2024-01-24)

主引用文献

Franceus, J.,Capra, N.,Desmet, T.,Thunnissen, A.W.H.
Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6 F -Phosphate Phosphorylase.
Int J Mol Sci, 20:-, 2019

PubMed Abstract: In family GH13 of the carbohydrate-active enzyme database, subfamily 18 contains glycoside phosphorylases that act on α-sugars and glucosides. Because their phosphorolysis reactions are effectively reversible, these enzymes are of interest for the biocatalytic synthesis of various glycosidic compounds. Sucrose 6-phosphate phosphorylases (SPPs) constitute one of the known substrate specificities. Here, we report the characterization of an SPP from with a far stricter specificity than the previously described promiscuous SPP from . Crystal structures of both SPPs were determined to provide insight into their similarities and differences. The residues responsible for binding the fructose 6-phosphate group in subsite +1 were found to differ considerably between the two enzymes. Furthermore, several variants that introduce a higher degree of substrate promiscuity in the strict SPP from were designed. These results contribute to an expanded structural knowledge of enzymes in subfamily GH13_18 and facilitate their rational engineering.

PubMed: 31405215
DOI: 10.3390/ijms20163906

実験手法

X-RAY DIFFRACTION (1.83 Å)