Lipoyl(octanoyl) transferase

In enzymology, a lipoyl(octanoyl) transferase (EC 2.3.1.181) is an enzyme that catalyzes the chemical reaction

octanoyl-[acyl-carrier-protein] + protein protein N6-(octanoyl)lysine + acyl carrier protein
Lipoyl(octanoyl) transferase
Identifiers
EC number2.3.1.181
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Thus, the two substrates of this enzyme are octanoyl-[acyl-carrier-protein] and protein, whereas its two products are protein N6-(octanoyl)lysine and acyl carrier protein.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase. Other names in common use include LipB, lipoyl (octanoyl)-[acyl-carrier-protein]-protein, N-lipoyltransferase, lipoyl (octanoyl)-acyl carrier protein:protein transferase, lipoate/octanoate transferase, lipoyltransferase, octanoyl-[acyl carrier protein]-protein N-octanoyltransferase, and lipoyl(octanoyl)transferase. This enzyme participates in lipoic acid metabolism.

References

    • Broadwater JA, Haas JA, Fox BG, Booker SJ (2005). "Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase". Protein Expr. Purif. 39 (2): 269–82. doi:10.1016/j.pep.2004.10.021. PMID 15642479.
    • 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.
    • 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.
    • 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.
    • Wada M, Yasuno R, Jordan SW, Cronan JE, Wada H (2001). "Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase". Plant Cell Physiol. 42 (6): 650–6. doi:10.1093/pcp/pce081. PMID 11427685.
    • Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69: 961–1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.


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