Lipoate–protein ligase

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Lipoate–protein ligase
EC number
CAS number 144114-18-1
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Lipoate–protein ligase (EC, LplA, lipoate protein ligase, lipoate–protein ligase A, LPL, LPL-B) is an enzyme with systematic name ATP:lipoate adenylyltransferase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

(1) ATP + lipoate diphosphate + lipoyl-AMP
(2) lipoyl-AMP + apoprotein protein N6-(lipoyl)lysine + AMP

This enzyme requires Mg2+ as a cofactor.


  1. ^ Morris, T.W.; Reed, K.E.; Cronan, J.E. (1994). "Identification of the gene encoding lipoate–protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product". J. Biol. Chem. 269 (23): 16091–16100. PMID 8206909. 
  2. ^ Green, D.E.; Morris, T.W.; Green, J.; Cronan, J.E.; Jr.; Guest, J.R. (1995). "Purification and properties of the lipoate protein ligase of Escherichia coli". Biochem. J. 309: 853–862. PMC 1135710Freely accessible. PMID 7639702. 
  3. ^ Zhao, X.; Miller, J.R.; Jiang, Y.; Marletta, M.A.; Cronan, J.E. (2003). "Assembly of the covalent linkage between lipoic acid and its cognate enzymes". Chem. Biol. 10: 1293–1302. doi:10.1016/j.chembiol.2003.11.016. PMID 14700636. 
  4. ^ Kim do, J.; Kim, K.H.; Lee, H.H.; Lee, S.J.; Ha, J.Y.; Yoon, H.J.; Suh, S.W. (2005). "Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains". J. Biol. Chem. 280 (45): 38081–38089. doi:10.1074/jbc.M507284200. PMID 16141198. 
  5. ^ Fujiwara, K.; Toma, S.; Okamura-Ikeda, K.; Motokawa, Y.; Nakagawa, A.; Taniguchi, H. (2005). "Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site". J. Biol. Chem. 280 (39): 33645–33651. doi:10.1074/jbc.M505010200. PMID 16043486. 
  6. ^ Jordan, S.W.; Cronan, J.E. (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): 17903–17906. doi:10.1074/jbc.272.29.17903. PMID 9218413. 
  7. ^ Perham, R.N. (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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