ITEM METADATA RECORD
Title: The role of 2-hydroxyacyl-CoA lyase, a thiamin pyrophosphate-dependent enzyme, in the peroxisomal metabolism of 3-methyl-branched fatty acids and 2-hydroxy straight-chain fatty acids
Authors: Casteels, Minne ×
Sniekers, Mieke
Fraccascia, Patrizia
Mannaerts, Guy
Van Veldhoven, Paul P #
Issue Date: 18-Oct-2007
Series Title: Biochemical Society transactions vol:35 issue:Pt 5 pages:876-880
Conference: Life sciences location:Glasgow date:July 2007
Abstract: 2-Hydroxyphytanoyl-CoA lyase (abbreviated as 2-HPCL), renamed to 2-hydroxyacyl-CoA lyase (abbreviated as HACL1), is the first peroxisomal enzyme in mammals that has been found to be dependent on TPP (thiamin pyrophosphate). It was discovered in 1999, when studying alpha-oxidation of phytanic acid. HACL1 has an important role in at least two pathways: (i) the degradation of 3-methyl-branched fatty acids like phytanic acid and (ii) the shortening of 2-hydroxy long-chain fatty acids. In both cases, HACL1 catalyses the cleavage step, which involves the splitting of a carbon-carbon bond between the first and second carbon atom in a 2-hydroxyacyl-CoA intermediate leading to the production of an (n-1) aldehyde and formyl-CoA. The latter is rapidly converted into formate and subsequently to CO(2). HACL1 is a homotetramer and has a PTS (peroxisomal targeting signal) at the C-terminal side (PTS1). No deficiency of HACL1 has been described yet in human, but thiamin deficiency might affect its activity.
URI: 
ISSN: 0300-5127
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Pharmacology Section (-)
Department of Pharmaceutical & Pharmacological Sciences - miscellaneous
Laboratory of Lipid Biochemistry and Protein Interactions
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy

 




All items in Lirias are protected by copyright, with all rights reserved.

© Web of science