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Literature summary for 2.4.1.129 extracted from
- Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli (2003), J. Bacteriol., 185, 5342-5348.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| construction of expression plasmids allowing the production of native PBP1B or PBP1B variants with an inactive transpeptidase or transglycosylase domain or both. Overproduction of the inactive PBP1B variants, but not of the active proteins, causes lysis of wild-type cells. Cells became tolerant to lysis by inactive PBP1B at a pH of 5.0 | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | overproduction of the inactive PBP1B variants causes lysis of wild-type cells | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | overproduction of the inactive PBP1B variants causes lysis of wild-type cells | Escherichia coli | ? | - |
? | |
| additional information | the penicillin-binding protein 1B is a bifunctional murein synthase containing both a transpeptidase domain and a transglycosylasedomain, The protein is present in three forms: alpha, beta and gamma | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PBP1b | - |
Escherichia coli |
| penicillin-binding protein 1B | - |
Escherichia coli |
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