LIAS
Function
Catalyzes 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, thereby converting the octanoylated domains into lipoylated derivatives.
Involvement in disease
Hyperglycinemia, lactic acidosis, and seizures
HGCLAS
An enzymatic defect resulting in an autosomal recessive disorder of mitochondrial metabolism. It is characterized by early-onset lactic acidosis, severe encephalomyopathy, and a pyruvate oxidation defect. Affected individuals have neonatal-onset epilepsy, poor growth, psychomotor retardation, muscular hypotonia, lactic acidosis, and elevated glycine concentration in plasma and urine.
None
The disease is caused by variants affecting the gene represented in this entry.
Pathway
Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Sequence Similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Cellular localization
- Mitochondrion
Alternative names
LAS, HUSSY-01, LIAS, Lipoate synthase, Lipoic acid synthase, LS, Lip-syn