LIAS
LIAS (lipoic acid synthetase, also known as LAS) is a mitochondrial iron-sulfur enzyme that catalyses the final step in the de novo biosynthesis of lipoic acid. It belongs to the radical SAM superfamily and the lipoyl synthase family. Browse Assay Genie's current range of LIAS research reagents below, or read on for the biology behind the target.
LIAS catalyses the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes. In doing so it converts octanoylated domains into their lipoylated derivatives. As the enzyme that performs the final step in the de novo pathway for lipoic acid biosynthesis, it underpins the supply of this cofactor, which is described as a potent antioxidant.
The protein is an iron-sulfur enzyme localised to the mitochondrion. It belongs to the radical S-adenosylmethionine (radical SAM) superfamily, which is also the HGNC gene group for the locus, and to the lipoyl synthase family. NCBI Gene places it within the biotin and lipoic acid synthetases family. The human LIAS gene is conserved in rodents, with mouse and rat orthologs both named Lias, which allows the enzyme to be studied in common model systems. Alternative splicing occurs at this locus, and several transcript variants encoding distinct isoforms have been identified.
Because lipoylation depends on this enzyme, LIAS is of interest in studies of mitochondrial metabolism. Deficient expression of the enzyme has been linked to conditions such as diabetes, atherosclerosis and neonatal-onset epilepsy. Researchers working on the LIAS protein or the LIAS gene often use it to examine lipoic acid biosynthesis and the modification of lipoate-dependent enzymes.
LIAS performs the final step of the de novo pathway, making it a central enzyme for studying how lipoic acid is produced.
The enzyme converts octanoylated lipoyl domains of lipoate-dependent enzymes into lipoylated forms, a modification relevant to mitochondrial protein function.
As an iron-sulfur radical SAM enzyme that inserts two sulfur atoms radically, LIAS is a model for this superfamily's chemistry.
Deficient LIAS expression has been linked to diabetes, atherosclerosis and neonatal-onset epilepsy, motivating disease-focused research.
LIAS catalyses the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl group on lipoyl domains of lipoate-dependent enzymes. This converts them to lipoylated derivatives and completes de novo lipoic acid biosynthesis in the mitochondrion.
LIAS is the HGNC symbol for lipoic acid synthetase, and LAS is a listed alias. UniProt names the protein lipoyl synthase, mitochondrial. NCBI Gene reports that alternative splicing occurs at this locus, giving several transcript variants that encode distinct isoforms.
NCBI Gene reports that deficient LIAS expression has been linked to diabetes, atherosclerosis and neonatal-onset epilepsy. Mouse and rat each have an ortholog named Lias; check the datasheet of any product for its validated reactivity.
Other lipoylation pathway enzymes, lipoate-dependent mitochondrial enzymes and radical SAM proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O43766; product specifications from Assay Genie datasheets.