- Both 6S- and 6R-lipoates can act as substrates but there is a
preference for the naturally occurring R-form.
- Selenolipoate, i.e. 5-(1,2-diselenolan-3-yl)pentanoic acid,
and 6-sulfanyloctanoate can also act as substrates, but more slowly.
- Responsible for lipoylation in the presence of exogenous lipoic acid.
- 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).
- Attaches lipoic acid to the lipoyl domains of these proteins.
- 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.
|
| UniProtKB/Swiss-Prot |
| A0KMH0, LPLA_AERHH; | Q9Y9E6, LPLA_AERPE; | A4SQ09, LPLA_AERS4; |
| P60809, LPLA_BDEBA; | Q7VR65, LPLA_BLOFL; | Q492U9, LPLA_BLOPB; |
| A8ALX2, LPLA_CITK8; | A7ZVS8, LPLA_ECO24; | P60776, LPLA_ECO57; |
| A8A8B4, LPLA_ECOHS; | A1AJV3, LPLA_ECOK1; | Q0T8S7, LPLA_ECOL5; |
| Q8FA49, LPLA_ECOL6; | B1IS33, LPLA_ECOLC; | P32099, LPLA_ECOLI; |
| Q1R257, LPLA_ECOUT; | A4W6A2, LPLA_ENT38; | A7MIG6, LPLA_ENTS8; |
| A6TI00, LPLA_KLEP7; | P47512, LPLA_MYCGE; | P75394, LPLA_MYCPN; |
| Q1QEC2, LPLA_PSYCK; | A9MRA3, LPLA_SALAR; | Q57G36, LPLA_SALCH; |
| Q5PK29, LPLA_SALPA; | A9N7E6, LPLA_SALPB; | Q8Z0U0, LPLA_SALTI; |
| Q8ZJV1, LPLA_SALTY; | O13629, LPLA_SCHPO; | A8GDS3, LPLA_SERP5; |
| Q31SV2, LPLA_SHIBS; | Q327K9, LPLA_SHIDS; | Q3YU08, LPLA_SHISS; |
| Q9HKT1, LPLA_THEAC; | A5F8E4, LPLA_VIBC3; | Q9KS71, LPLA_VIBCH; |
| P47051, LPLA_YEAST; | A1JPK8, LPLA_YERE8; | A7FHI0, LPLA_YERP3; |
| Q1C748, LPLA_YERPA; | Q8ZDY2, LPLA_YERPE; | Q1CII3, LPLA_YERPN; |
| A4TIN0, LPLA_YERPP; | Q66A10, LPLA_YERPS; |
|