University of Oulu

Kind, L., Kursula, P. Structural properties and role of the endocannabinoid lipases ABHD6 and ABHD12 in lipid signalling and disease. Amino Acids 51, 151–174 (2019).

Structural properties and role of the endocannabinoid lipases ABHD6 and ABHD12 in lipid signalling and disease

Saved in:
Author: Kind, Laura1; Kursula, Petri1,2
Organizations: 1Department of Biomedicine, University of Bergen, Bergen, Norway
2Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 3 MB)
Persistent link:
Language: English
Published: Springer Nature, 2018
Publish Date: 2021-03-04


The endocannabinoid (eCB) system is an important part of both the human central nervous system (CNS) and peripheral tissues. It is involved in the regulation of various physiological and neuronal processes and has been associated with various diseases. The eCB system is a complex network composed of receptor molecules, their cannabinoid ligands, and enzymes regulating the synthesis, release, uptake, and degradation of the signalling molecules. Although the eCB system and the molecular processes of eCB signalling have been studied extensively over the past decades, the involved molecules and underlying signalling mechanisms have not been described in full detail. An example pose the two poorly characterised eCB-degrading enzymes α/β-hydrolase domain protein six (ABHD6) and ABHD12, which have been shown to hydrolyse 2-arachidonoyl glycerol—the main eCB in the CNS. We review the current knowledge about the eCB system and the role of ABHD6 and ABHD12 within this important signalling system and associated diseases. Homology modelling and multiple sequence alignments highlight the structural features of the studied enzymes and their similarities, as well as the structural basis of disease-related ABHD12 mutations. However, homologies within the ABHD family are very low, and even the closest homologues have widely varying substrate preferences. Detailed experimental analyses at the molecular level will be necessary to understand these important enzymes in full detail.

see all

Series: Amino acids
ISSN: 0939-4451
ISSN-E: 1438-2199
ISSN-L: 0939-4451
Volume: 51
Issue: 2
Pages: 151 - 174
DOI: 10.1007/s00726-018-2682-8
Type of Publication: A2 Review article in a scientific journal
Field of Science: 1182 Biochemistry, cell and molecular biology
Funding: This study was supported by a training grant from the ERASMUS + programme.
Copyright information: © Springer-Verlag GmbH Austria, part of Springer Nature 2018. This is a post-peer-review, pre-copyedit version of an article published in Amino Acids. The final authenticated version is available online at: