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Literature summary for 5.6.2.1 extracted from
- Native state dynamics and mechanical properties of human topoisomerase I within a structure-based coarse-grained model (2009), Proteins, 77, 420-431.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P11387 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Topo I catalyses two distinct reactions, the DNA relaxation and the phosphorylation of serine/arginine motifs which are present in essential splicing factors in a mutually exclusive manner, structure-function relationship, molecular dynamics modelling, overview | Homo sapiens | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | structure-function relationship, molecular dynamics modelling, detailed overview. Topo I is a single polypeptide of 765 amino acid residues comprising four domains called: N-terminal domain with residues M1-G214, core domain with I215-A635, linker domain with P636-K712, and C-terminal domain with Q713-F765 domain. The core domain is further divided into three subdomains that form two distinct lobes in the three-dimensional structure of topo I: the cap region, including subdomains I formed by residues I215-E232 and S320-S433, subdomain II formed by residues P233-M319, and the separate subdomain III consisting of residues R434-A635 | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Topoisomerase I | - |
Homo sapiens |
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