7C91

Blasnase-T13A with D-asn

7C91 の概要

• エントリーDOI: 10.2210/pdb7c91/pdb
• 分子名称: L-asparaginase, D-ASPARAGINE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: substrate, complex, mutant, hydrolase
• 由来する生物種: Bacillus paralicheniformis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83307.22

構造登録者

Lu, F.,Ran, T.,Jiao, L.,Wang, W. (登録日: 2020-06-04, 公開日: 2021-06-09, 最終更新日: 2023-11-29)

主引用文献

Ran, T.,Jiao, L.,Wang, W.,Chen, J.,Chi, H.,Lu, Z.,Zhang, C.,Xu, D.,Lu, F.
Structures of l-asparaginase from Bacillus licheniformis Reveal an Essential Residue for its Substrate Stereoselectivity.
J.Agric.Food Chem., 69:223-231, 2021

PubMed Abstract: l-Asparaginase, which catalyzes the hydrolysis of l-asparagine, is an important enzyme in both the clinical and food industry. Exploration of efficient l-asparaginase with high substrate specificity, especially high chiral selectivity, is essential for extending its use. Herein, various crystal structures of type I l-asparaginase from (BlAsnase) have been resolved, and we found that there are two additional tyrosines in BlAsnase, contributing to the binding and catalysis of d-asparagine. Strikingly, the substitution of Tyr278 with methionine impaired the interaction with d-asparagine via water molecules due to the small hydrophobic side chain of methionine, which forced the ligand to the deep side of the active site toward the catalytic residues and thus resulted in the loss of hydrolyzing function. Our investigation of the substrate recognition mechanism of BlAsnase is significant for both a better understanding of l-asparaginase and its rational design to achieve high specificity for clinical and industrial applications.

PubMed: 33371681
DOI: 10.1021/acs.jafc.0c06609

実験手法

X-RAY DIFFRACTION (1.98 Å)