Both 6S-and 6R-lipoates can act as substrates but there is a preference for the naturally occurring R-form.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Attaches lipoic acid to the lipoyl domains of these proteins.,
Both 6S-and 6R-lipoates can act as substrates but there is a preference for the naturally occurring R-form.,
It is likely that an alternative pathway, involving EC 2.3.1.181 and EC 2.8.1.8 is the normal route for lipoylation.,
Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).,
Responsible for lipoylation in the presence of exogenous lipoic acid.,
Selenolipoate, i.e. 5-(1,2-diselenolan-3-yl)pentanoic acid, and 6-sulfanyloctanoate can also act as substrates, but more slowly.
|
| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
LPL,
Lipoate protein ligase,
Lipoate--protein ligase,
Lipoate-protein ligase A
|
| uniprot:activity |
(1) ATP + lipoate = diphosphate + lipoyl-AMP.,
(2) Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP.
|
| uniprot:cofactor |
Magnesium
|