http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID319742
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | lipoate-protein ligase. Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein. |
| title | LplA |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32065227 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22553371 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27373413 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28137419 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1054763 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/171731 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
| Predicate | Subject |
|---|---|
| has component | http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9Y234 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCO46419 http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8VCM4 |
Total number of triples: 12.