EC number:6.3.1.20

Enzyme

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     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases)
ID:6.3.1.20
Description:Lipoate--protein ligase.
Alternative Name: LPL.
Lipoate-protein ligase A.
Lipoate protein ligase.
Cath: 3.30.390.50; 3.30.930.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 6.3.1.20
BRENDA Enzyme Link: BRENDA 6.3.1.20
KEGG Enzyme Link: KEGG6.3.1.20
BioCyc Enzyme Link: BioCyc 6.3.1.20
ExPASy Enzyme Link: ExPASy6.3.1.20
EC2PDB Enzyme Link: EC2PDB 6.3.1.20
ExplorEnz Enzyme Link: ExplorEnz 6.3.1.20
PRIAM enzyme-specific profiles Link: PRIAM 6.3.1.20
IntEnz Enzyme Link: IntEnz 6.3.1.20
MEDLINE Enzyme Link: MEDLINE 6.3.1.20

EC number:6.3.1.20

MSA:

6.3.1.20;
Phylogenetic Tree:

6.3.1.20;
Uniprot:
M-CSA:
RHEA:49288 (R)-lipoate + [lipoyl-carrier protein]-L-lysine + ATP = [lipoyl-carrier protein]-(R)-N(6)-lipoyl-L-lysine + AMP + diphosphate + H(+)
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[O;H0;+0:4]-[P;H0;+0:5](-[*:6])(=[*:7])-[*:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:3]-[OH;+0:4].[*:6]-[P;H0;+0:5](=[*:7])(-[*:8])-[OH;+0:12].[*:9]=[C;H0;+0:10](-[*:11])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria.Jordan SW, Cronan JE Jr1997 Jul 189218413
Purification and properties of the lipoate protein ligase of Escherichia coli.Green DE, Morris TW, Green J, Cronan JE Jr, Guest JR1995 Aug 17639702
A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis.Martin N, Christensen QH, Mansilla MC, Cronan JE, de Mendoza D2011 Apr21338420
Assembly of the covalent linkage between lipoic acid and its cognate enzymes.Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE2003 Dec14700636
Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP.Fujiwara K, Hosaka H, Matsuda M, Okamura-Ikeda K, Motokawa Y, Suzuki M, Nakagawa A, Taniguchi H2007 Aug 317570395
Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains.Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW2005 Nov 1116141198
Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H2005 Sep 3016043486
Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.Perham RN200010966480
Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product.Morris TW, Reed KE, Cronan JE Jr1994 Jun 108206909
Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, Peleg AY, Leys D, Traven A, Ahel I2015 Jul 1626166706
A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins.Posner MG, Upadhyay A, Bagby S, Hough DW, Danson MJ2009 Aug19594830
The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases.Christensen QH, Cronan JE2009 Aug 719520844