Lipoyl amidotransferase
| Lipoyl amidotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.200 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Lipoyl amidotransferase (EC 2.3.1.200, LipL (gene)) is an enzyme with systematic name (glycine cleavage system H)-N6-lipoyl-L-lysine:(lipoyl-carrier protein)-N6-L-lysine lipoyltransferase.[1] This enzyme catalyses the following chemical reaction
- [glycine cleavage system H]-N6-lipoyl-L-lysine + [lipoyl-carrier protein] glycine cleavage system H + [lipoyl-carrier protein]-N6-lipoyl-L-lysine
In the bacterium Listeria monocytogenes the enzyme takes part in a pathway for scavenging of lipoic acid.
References
[edit]- ^ Christensen QH, Hagar JA, O'Riordan MX, Cronan JE (September 2011). "A complex lipoate utilization pathway in Listeria monocytogenes". The Journal of Biological Chemistry. 286 (36): 31447–56. doi:10.1074/jbc.m111.273607. PMC 3173067. PMID 21768091.
External links
[edit]- Lipoyl+amidotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
