EC 6.3.1.20 - Lipoate—protein ligase

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IntEnz Enzyme Nomenclature
EC 6.3.1.20

Names

Accepted name:
lipoate—protein ligase
Other names:
lplA (gene name)
lipoate protein ligase
lipoate-protein ligase A
LPL
LPL-B
lplJ (gene name)
Systematic name:
[lipoyl-carrier protein]-L-lysine:lipoate ligase (AMP-forming)

Reaction

Cofactor

Comments:

Requires Mg2+. This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid [7]. The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [6]. Lipoylation is essential for the function of these enzymes. The enzyme can also use octanoate instead of lipoate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (80) [show] [UniProt]

References

  1. Morris, T.W., Reed, K.E. and Cronan, J.E., Jr.
    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 (1994). [PMID: 8206909]
  2. Green, D.E., Morris, T.W., Green, J., Cronan, J.E., Jr. and Guest, J.R.
    Purification and properties of the lipoate protein ligase of Escherichia coli.
    Biochem. J. 309: 853-862 (1995). [PMID: 7639702]
  3. Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and Cronan, J.E., Jr.
    Assembly of the covalent linkage between lipoic acid and its cognate enzymes.
    Chem. Biol. 10: 1293-1302 (2003). [PMID: 14700636]
  4. Kim, D.J., Kim, K.H., Lee, H.H., Lee, S.J., Ha, J.Y., Yoon, H.J. and Suh, S.W.
    Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains.
    J. Biol. Chem. 280: 38081-38089 (2005). [PMID: 16141198]
  5. Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A. and Taniguchi, H.
    Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.
    J. Biol. Chem. 280: 33645-33651 (2005). [PMID: 16043486]
  6. Jordan, S.W., Cronan, J.E., Jr.
    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 (1997). [PMID: 9218413]
  7. Perham, R.N.
    Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
    Annu. Rev. Biochem. 69: 961-1004 (2000). [PMID: 10966480]

[EC 6.3.1.20 created 2006 as EC 2.7.7.63, transferred 2016 to EC 6.3.1.20]