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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

Target type

Proteins

Primary research area

Metabolism

Molecular weight

41911Da

We found 2 products in 1 category

Primary Antibodies

Target

Application

Reactive species

Search our catalogue for 'LIAS' (2)

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