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Lipoat—protein ligaza

С Википедије, слободне енциклопедије
(преусмерено са Lipoat---protein ligaza)
Lipoat—protein ligaza
Identifikatori
EC broj2.7.7.63
CAS broj144114-18-1
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

Lipoat—protein ligaza (EC 2.7.7.63, LplA, lipoat proteinska ligaza, lipoat-proteinska ligaza A, LPL, LPL-B) je enzim sa sistematskim imenom ATP:lipoat adenililtransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju

(1) ATP + lipoat difosfat + lipoil-AMP
(2) lipoil-AMP + apoprotein protein N6-(lipoil)lizin + AMP

Za rad ovog enzima je neophodan jon Mg2+.

  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: 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. 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: 38081—38089. 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: 33645—33651. PMID 16043486. 
  6. ^ Jordan, S.W. & 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: 17903—17906. 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. PMID 10966480. 

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