Lipoate—protein ligase

From Wikipedia, the free encyclopedia
  (Redirected from Lipoate protein ligase)
Jump to: navigation, search
Lipoate—protein ligase
Identifiers
EC number 2.7.7.63
CAS number 144114-18-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Lipoate—protein ligase (EC 2.7.7.63, LplA, lipoate protein ligase, lipoate-protein ligase A, LPL, LPL-B) is an enzyme with system name ATP:lipoate adenylyltransferase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

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

This enzyme requires Mg2+ as a cofactor.

References[edit]

  1. ^ Morris, T.W., Reed, K.E. and Cronan, J.E., Jr. (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. and Guest, J.R. (1995). "Purification and properties of the lipoate protein ligase of Escherichia coli". Biochem. J. 309: 853–862. PMID 7639702. 
  3. ^ Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and 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. and 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. and 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. and Cronan, J.E., Jr. (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. 

External links[edit]