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Literature summary for 2.3.1.136 extracted from
- Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r (2008), Biochemistry, 47, 2312-2324.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a C-terminal hexahistidine tagged fusion protein | Neisseria meningitidis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D359A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| D371A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| D376A | mutant shows no enzymatic activity | Neisseria meningitidis |
| DELTA1-103 | mutant lacking the first 103 amino acids: after purification mutant is found as a monomer, indicating that dimerization of OatC depends on the first 34 amino acids. Mutant shows no activity | Neisseria meningitidis |
| DELTA1-34 | mutant lacking the first 34 amino acids: after purification mutant is found as a monomer, indicating that dimerization of OatC depends on the first 34 amino acids. Mutant retains 25% activity | Neisseria meningitidis |
| E336A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| E345A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| E379A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| H111A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| H183A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| H267A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| H31A | mutant shows enzymatic activity comparable to wild-type | Neisseria meningitidis |
| H399A | mutant shows no enzymatic activity | Neisseria meningitidis |
| H456A | mutant shows reduced enzymatic activity, 70% of wild-type level | Neisseria meningitidis |
| S285A | mutant retains 80% of wild-type activity | Neisseria meningitidis |
| S286A | mutant shows no enzymatic activity | Neisseria meningitidis |
| S286C | mutant shows no enzymatic activity | Neisseria meningitidis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 54000 | - |
SDS-PAGE, the first 34 amino acids form an efficient oligomerization domain, 2 * 54000 Da | Neisseria meningitidis |
| 54300 | - |
SDS-PAGE | Neisseria meningitidis |
| 105000 | - |
gel filtration | Neisseria meningitidis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Neisseria meningitidis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using a HisTrap HP column and a a Superdex 200 HR 10/30 column. FInal yield: 24 mg of enzyme from 500 ml of bacterial culture | Neisseria meningitidis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | no enzymatic activity is detected for free Neu5Ac and CMP-Neu5Ac, indicating that OatC is specific for oligo- or polySia. Since only Neisseria meningitidis serogroup C capsular polysaccharide (NmC-CPS) serves as an acceptor, this demonstrates that OatC is highly specific for alpha2,9-linked polySia | Neisseria meningitidis | ? | - |
? |  |
| Neisseria meningitidis serogroup C capsular polysaccharide + acetyl-CoA | relative activity: 100% | Neisseria meningitidis | ? | - |
? | |
| Neisseria meningitidis serogroup C capsular polysaccharide + propionyl-CoA | relative activity: 21.4% | Neisseria meningitidis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | SDS-PAGE, the first 34 amino acids form an efficient oligomerization domain, 2 * 54000 Da | Neisseria meningitidis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OatC | - |
Neisseria meningitidis |
| polysialic-acid O-acetyltransferase | - |
Neisseria meningitidis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Neisseria meningitidis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Neisseria meningitidis |
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Release 2023.1 (January 2023)
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