Biology:Lipoate–protein ligase
From HandWiki
| Lipoate–protein ligase | |||||||||
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| 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 | ||||||||
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Lipoate–protein ligase (EC 2.7.7.63, LplA, lipoate protein ligase, lipoate–protein ligase A, LPL, LPL-B) is an enzyme with systematic name ATP:lipoate adenylyltransferase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- (1) ATP + lipoate [math]\displaystyle{ \rightleftharpoons }[/math] diphosphate + lipoyl-AMP
- (2) lipoyl-AMP + apoprotein [math]\displaystyle{ \rightleftharpoons }[/math] protein N6-(lipoyl)lysine + AMP
This enzyme requires Mg2+ as a cofactor.
References
- ↑ "Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product". The Journal of Biological Chemistry 269 (23): 16091–100. June 1994. PMID 8206909.
- ↑ "Purification and properties of the lipoate protein ligase of Escherichia coli". The Biochemical Journal 309 (3): 853–62. August 1995. doi:10.1042/bj3090853. PMID 7639702.
- ↑ "Assembly of the covalent linkage between lipoic acid and its cognate enzymes". Chemistry & Biology 10 (12): 1293–302. December 2003. doi:10.1016/j.chembiol.2003.11.016. PMID 14700636.
- ↑ "Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains". The Journal of Biological Chemistry 280 (45): 38081–9. November 2005. doi:10.1074/jbc.M507284200. PMID 16141198.
- ↑ "Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site". The Journal of Biological Chemistry 280 (39): 33645–51. September 2005. doi:10.1074/jbc.M505010200. PMID 16043486.
- ↑ "A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria". The Journal of Biological Chemistry 272 (29): 17903–6. July 1997. doi:10.1074/jbc.272.29.17903. PMID 9218413.
- ↑ "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annual Review of Biochemistry 69: 961–1004. 2000. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.
External links
- Lipoate---protein+ligase at the US National Library of Medicine Medical Subject Headings (MeSH)
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