Lipoyl synthase

Lipoyl synthase
Identifiers
EC number	2.8.1.8
CAS number	189398-80-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a lipoyl synthase (EC 2.8.1.8) is an enzyme that catalyzes the chemical reaction

protein N₆-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine $\rightleftharpoons$ protein N₆-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine

The 3 substrates of this enzyme are protein N6-(octanoyl)lysine, sulfur, and S-adenosyl-L-methionine, whereas its 3 products are protein N6-(lipoyl)lysine, L-methionine, and 5'-deoxyadenosine.

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. This enzyme participates in lipoic acid metabolism, where it performs the final step in lipoic acid biosynthesis.

Nomenclature

The systematic name of this enzyme class is protein N6-(octanoyl)lysine:sulfur sulfurtransferase. Other names in common use include:

• LS,
• LipA,
• lipoate synthase, and
• protein 6-N-(octanoyl)lysine:sulfur sulfurtransferase.

References

• Cicchillo RM, Booker SJ (2005). "Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide". J. Am. Chem. Soc. 127 (9): 2860–1. doi:10.1021/ja042428u. PMID 15740115.
• Vanden Boom TJ, Reed KE, Cronan JE (1991). "Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system". J. Bacteriol. 173 (20): 6411–20. PMC 208974. PMID 1655709.
• Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE (2003). "Assembly of the covalent linkage between lipoic acid and its cognate enzymes". Chem. Biol. 10 (12): 1293–302. doi:10.1016/j.chembiol.2003.11.016. PMID 14700636.
• Souder MG, Tu L, Booker SJ (2004). "Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid". Biochemistry. 43 (21): 6378–86. doi:10.1021/bi049528x. PMID 15157071.
• Jordan SW, Cronan JE (1997). "A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria". J. Biol. Chem. 272 (29): 17903–6. doi:10.1074/jbc.272.29.17903. PMID 9218413.
• Broderick JB, Cronan JE, Marletta MA (2000). "Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein". Biochemistry. 39 (49): 15166–78. doi:10.1021/bi002060n. PMID 11106496.
• Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69 (1): 961–1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.