| EC |
3.5.1.138 |
| Accepted name: |
lipoamidase |
| Reaction: |
a [lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine + H2O = a [lipoyl-carrier protein]-L-lysine + (R)-lipoate |
| Other name(s): |
pyruvate dehydrogenase inactivase |
| Systematic name: |
[lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine amidohydrolase |
| Comments: |
The enzyme, characterized from the bacterium Enterococcus faecalis, is a member of the Ser-Ser-Lys triad amidohydrolase family. cf. EC 2.3.1.313, NAD-dependent lipoamidase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Reed, L.J., Koike, M., Levitch, M.E., Leach, F.R. Studies on the nature and reactions of protein-bound lipoic acid. J. Biol. Chem. 232 (1958) 143–158. [DOI] [PMID: 13549405] |
| 2. |
Suzuki, K, Reed L.J. Lipoamidase. J. Biol. Chem. 238 (1963) 4021–4025. [DOI] [PMID: 14086741] |
| 3. |
Jiang, Y. and Cronan, J.E. Expression cloning and demonstration of Enterococcus faecalis lipoamidase (pyruvate dehydrogenase inactivase) as a Ser-Ser-Lys triad amidohydrolase. J. Biol. Chem. 280 (2005) 2244–2256. [DOI] [PMID: 15528186] |
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| [EC 3.5.1.138 created 2023] |
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