Active site loop conformation regulates promiscuous activity in a lactonase from Geobacillus kaustophilus HTA426.

Active site loop conformation regulates promiscuous activity in a lactonase from Geobacillus kaustophilus HTA426.

Enzyme promiscuity is a prerequisite for fast divergent evolution of biocatalysts. A phosphotriesterase-like lactonase (PLL) from Geobacillus kaustophilus HTA426 (GkaP) exhibits main lactonase and promiscuous phosphotriesterase activities. To understand its catalytic and evolutionary mechanisms, we...

Full description

Saved in:
Bibliographic Details
Main Authors: Yu Zhang, Jiao An, Guang-Yu Yang, Aixi Bai, Baisong Zheng, Zhiyong Lou, Geng Wu, Wei Ye, Hai-Feng Chen, Yan Feng, Giuseppe Manco
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0115130&type=printable
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items

Similar Items