Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 2.7.7.63

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.7.7.63

Enzymes and Genes:
lipoyl-protein ligase A Inferred from experiment : lplA ( Escherichia coli K-12 substr. MG1655 )
lipoate-protein ligase Inferred from experiment : lplJ ( Bacillus subtilis subtilis 168 )
lipoate-protein ligase A Inferred from experiment : lplA , lplB ( Thermoplasma acidophilum )

In Pathway: lipoate salvage I

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: lipoate—protein ligase

Enzyme Commission Synonyms: LplA, lipoate protein ligase, lipoate-protein ligase A, LPL, LPL-B

Standard Gibbs Free Energy (ΔrG in kcal/mol): -85.63157 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Requires Mg2+. Both 6S- and 6R-lipoates can act as substrates but there is a preference for the naturally occurring R-form. Selenolipoate, i.e. 5-(1,2-diselenolan-3-yl)pentanoic acid, and 6-sulfanyloctanoate can also act as substrates, but more slowly [Green95]. Responsible for lipoylation in the presence of exogenous lipoic acid. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [Jordan97a]. Attaches lipoic acid to the lipoyl domains of these proteins. It is likely that an alternative pathway, involving EC 2.3.1.181 and EC 2.8.1.8 is the normal route for lipoylation [Perham00].

Citations: [Morris94, Zhao03, Kim05, Fujiwara05]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R07771

Relationship Links: BRENDA:EC:2.7.7.63 , ENZYME:EC:2.7.7.63 , IUBMB-ExplorEnz:EC:2.7.7.63


References

Fujiwara05: 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);33645-51. PMID: 16043486

Green95: Green DE, Morris TW, Green J, Cronan JE, Guest JR (1995). "Purification and properties of the lipoate protein ligase of Escherichia coli." Biochem J 309 ( Pt 3);853-62. PMID: 7639702

Jordan97a: Jordan SW, Cronan JE (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);17903-6. PMID: 9218413

Kim05: Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW (2005). "Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains." J Biol Chem 280(45);38081-9. PMID: 16141198

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Morris94: Morris TW, Reed KE, Cronan JE (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);16091-100. PMID: 8206909

Perham00: Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions." Annu Rev Biochem 69;961-1004. PMID: 10966480

Zhao03: Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE (2003). "Assembly of the covalent linkage between lipoic acid and its cognate enzymes." Chem Biol 10(12);1293-302. PMID: 14700636


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 27, 2014, biocyc11.