6JQ9

Crystal structure of a lyase from Alteromonas sp.

6JQ9 の概要

• エントリーDOI: 10.2210/pdb6jq9/pdb
• 分子名称: Short ulvan lyase, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Alteromonas sp. LOR
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 110299.31

構造登録者

Qin, H.M.,Guo, Q.Q. (登録日: 2019-03-29, 公開日: 2020-04-01, 最終更新日: 2024-05-29)

主引用文献

Qin, H.M.,Gao, D.,Zhu, M.,Li, C.,Zhu, Z.,Wang, H.,Liu, W.,Tanokura, M.,Lu, F.
Biochemical characterization and structural analysis of ulvan lyase from marine Alteromonas sp. reveals the basis for its salt tolerance.
Int.J.Biol.Macromol., 147:1309-1317, 2020

PubMed Abstract: Marine macroalgae have gained considerable attention as renewable biomass sources. Ulvan is a water-soluble anionic polysaccharide, and its depolymerization into fermentable monosaccharides has great potential for the production of bioethanol or high-value food additives. Ulvan lyase from Alteromonas sp. (AsPL) utilizes a β-elimination mechanism to cleave the glycosidic bond between rhamnose 3-sulfate and glucuronic acid, forming an unsaturated uronic acid at the non-reducing end. AsPL was active in the temperature range of 30-50 °C and pH values ranging from 7.5 to 9.5. Furthermore, AsPL was found to be halophilic, showing high activity and stability in the presence of up to 2.5 M NaCl. The apparent K and k values of AsPL are 3.19 ± 0.37 mg mL and 4.19 ± 0.21 s, respectively. Crystal structure analysis revealed that AsPL adopts a β-propeller fold with four anti-parallel β-strands in each of the seven propeller blades. The acid residues at the protein surface and two Ca coordination sites contribute to its salt tolerance. The research on ulvan lyase has potential commercial value in the utilization of algal resources for biofuel production to relieve the environmental burden of petrochemicals.

PubMed: 31751708
DOI: 10.1016/j.ijbiomac.2019.10.095

実験手法

X-RAY DIFFRACTION (1.81 Å)