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Literature summary for 6.3.1.20 extracted from
- Chlamydia trachomatis serovar L2 can utilize exogenous lipoic acid through the action of the lipoic acid ligase LplA1 (2010), J. Bacteriol., 192, 6172-6181.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Chlamydia trachomatis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chlamydia trachomatis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | recombinant LplA1Ct is able to lipoylate apo-PDH and 2-OGDH-E2 subunits purified from Escherichia coli ATM967 as detected by Western blotting with anti-lipoic acid antibody. LplA1Ct is also able to lipoylate the recombinant chlamydial BCKDH-E2 subunit | Chlamydia trachomatis | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lipoic acid ligase | - |
Chlamydia trachomatis |
| LplA1Ct | - |
Chlamydia trachomatis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Chlamydia trachomatis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Chlamydia trachomatis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | LplA1Ct is able to complement an Escherichia coli LplA knockout mutant at an efficiency of 94% | Chlamydia trachomatis |
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Release 2023.1 (January 2023)
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