Biology:Lipoyl(octanoyl) transferase
Lipoyl(octanoyl) transferase | |||||||||
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Identifiers | |||||||||
EC number | 2.3.1.181 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a lipoyl(octanoyl) transferase (EC 2.3.1.181) is an enzyme that catalyzes the chemical reaction
- octanoyl-[acyl-carrier-protein] + protein [math]\displaystyle{ \rightleftharpoons }[/math] protein N6-(octanoyl)lysine + acyl carrier protein
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
- "Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase". Protein Expr. Purif. 39 (2): 269–82. 2005. doi:10.1016/j.pep.2004.10.021. PMID 15642479.
- "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. 1991. PMID 1655709.
- "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. 1997. doi:10.1074/jbc.272.29.17903. PMID 9218413.
- "Assembly of the covalent linkage between lipoic acid and its cognate enzymes". Chem. Biol. 10 (12): 1293–302. 2003. doi:10.1016/j.chembiol.2003.11.016. PMID 14700636.
- "Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase". Plant Cell Physiol. 42 (6): 650–6. 2001. 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.
![]() | Original source: https://en.wikipedia.org/wiki/Lipoyl(octanoyl) transferase.
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