Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated From Erythrobacter longus

• Published in: Frontiers in microbiology Vol. 12; p. 798194
• Main Authors: Ding, Yi, Nie, Laiyin, Yang, Xiao-Chen, Li, Yang, Huo, Ying-Yi, Li, Zhengyang, Gao, Yan, Cui, Heng-Lin, Li, Jixi, Xu, Xue-Wei
• Format: Journal Article
• Language: English
• Published: Switzerland Frontiers Media S.A 05.01.2022
• Subjects: catalytic pocket; crystal structure; enzyme mutation; Microbiology; pH regulation; serine esterase; crystal structure; catalytic pocket; pH regulation; serine esterase; enzyme mutation

Esterases are a class of enzymes that split esters into an acid and an alcohol in a chemical reaction with water, having high potential in pharmaceutical, food and biofuel industrial applications. To advance the understanding of esterases, we have identified and characterized E53, an alkalophilic es...