(Redirected from
ATP:lipoate adenylyltransferase)
| Lipoate–protein ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.63 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 diphosphate + lipoyl-AMP
- (2) lipoyl-AMP + apoprotein protein N6-(lipoyl)lysine + AMP
This enzyme requires Mg2+ as a cofactor.
References
- ^ Morris TW, Reed KE, Cronan JE (June 1994). "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. PMID 8206909.
- ^ Green DE, Morris TW, Green J, Cronan JE, Guest JR (August 1995). "Purification and properties of the lipoate protein ligase of Escherichia coli". The Biochemical Journal. 309 (3): 853–62. doi: 10.1042/bj3090853. PMC 1135710. PMID 7639702.
- ^ Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE (December 2003). "Assembly of the covalent linkage between lipoic acid and its cognate enzymes". Chemistry & Biology. 10 (12): 1293–302. doi: 10.1016/j.chembiol.2003.11.016. PMID 14700636.
- ^ Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW (November 2005). "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. doi: 10.1074/jbc.M507284200. PMID 16141198.
- ^ Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H (September 2005). "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. doi: 10.1074/jbc.M505010200. PMID 16043486.
- ^ Jordan SW, Cronan JE (July 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". The Journal of Biological Chemistry. 272 (29): 17903–6. doi: 10.1074/jbc.272.29.17903. PMID 9218413.
- ^ Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annual Review of Biochemistry. 69: 961–1004. doi: 10.1146/annurev.biochem.69.1.961. PMID 10966480.
External links
- Lipoate---protein+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
(Redirected from
ATP:lipoate adenylyltransferase)
| Lipoate–protein ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.63 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 diphosphate + lipoyl-AMP
- (2) lipoyl-AMP + apoprotein protein N6-(lipoyl)lysine + AMP
This enzyme requires Mg2+ as a cofactor.
References
- ^ Morris TW, Reed KE, Cronan JE (June 1994). "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. PMID 8206909.
- ^ Green DE, Morris TW, Green J, Cronan JE, Guest JR (August 1995). "Purification and properties of the lipoate protein ligase of Escherichia coli". The Biochemical Journal. 309 (3): 853–62. doi: 10.1042/bj3090853. PMC 1135710. PMID 7639702.
- ^ Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE (December 2003). "Assembly of the covalent linkage between lipoic acid and its cognate enzymes". Chemistry & Biology. 10 (12): 1293–302. doi: 10.1016/j.chembiol.2003.11.016. PMID 14700636.
- ^ Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW (November 2005). "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. doi: 10.1074/jbc.M507284200. PMID 16141198.
- ^ Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H (September 2005). "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. doi: 10.1074/jbc.M505010200. PMID 16043486.
- ^ Jordan SW, Cronan JE (July 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". The Journal of Biological Chemistry. 272 (29): 17903–6. doi: 10.1074/jbc.272.29.17903. PMID 9218413.
- ^ Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annual Review of Biochemistry. 69: 961–1004. doi: 10.1146/annurev.biochem.69.1.961. PMID 10966480.
External links
- Lipoate---protein+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)