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Literature summary for 6.3.1.20 extracted from
- The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains (2015), J. Biol. Chem., 290, 7280-7290.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in an Escherichia coli ligase-deficient strain QC146 | Streptomyces coelicolor |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
x * 40000, SDS-PAGE | Streptomyces coelicolor |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces coelicolor | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + (R)-lipoate | - |
Streptomyces coelicolor | lipoyl-AMP + diphosphate | - |
r |  |
| lipoyl-AMP + [glycine cleavage H protein]-L-lysine | - |
Streptomyces coelicolor | [glycine cleavage H protein]-N6-(lipoyl)lysine + AMP | - |
ir | |
| lipoyl-AMP + [lE2p subunit of the pyruvate dehydrogenase complex]-L-lysine | - |
Streptomyces coelicolor | [E2p subunit of the pyruvate dehydrogenase complex]-N6-(lipoyl)lysine + AMP | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, SDS-PAGE | Streptomyces coelicolor |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lipoate ligase | - |
Streptomyces coelicolor |
| LPLA | - |
Streptomyces coelicolor |
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Release 2023.1 (January 2023)
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