Lan_2021_J.Chem.Inf.Model__

Reference

Title : Glycerol is Released from a New Path in MGL Lipase Catalytic Process - Lan_2021_J.Chem.Inf.Model__
Author(s) : Lan D , Li S , Tang W , Zhao Z , Luo M , Yuan S , Xu J , Wang Y
Ref : J Chem Inf Model , : , 2021
Abstract : Traditionally, it is believed that the substrate and products of a monoacylglycerol lipase (MGL) share the same path to enter and exit the catalytic site. Glycerol (a product of MGL), however, was recently hypothesized to be released through a different path. In order to improve the catalytic efficacy and thermo-stability of MGL, it is important to articulate the pathways of a MGL products releasing. In this study, with structure biological approaches, biochemical experiments, and in silico methods, we prove that glycerol is released from a different path in the catalytic site indeed. The fatty acid (another product of MGL) does share the same binding path with the substrate. This discovery paves a new road to design MGL inhibitors or optimize MGL catalytic efficacy.
ESTHER : Lan_2021_J.Chem.Inf.Model__
PubMedSearch : Lan_2021_J.Chem.Inf.Model__
PubMedID: 34873908

Related information

Citations formats

Lan D, Li S, Tang W, Zhao Z, Luo M, Yuan S, Xu J, Wang Y (2021)
Glycerol is Released from a New Path in MGL Lipase Catalytic Process
J Chem Inf Model :

Lan D, Li S, Tang W, Zhao Z, Luo M, Yuan S, Xu J, Wang Y (2021)
J Chem Inf Model :