Any feedback?
Literature summary for 2.1.1.8 extracted from
- The histamine N-methyltransferase T105I polymorphism affects active site structure and dynamics (2008), Biochemistry, 47, 893-901.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| T105I | common threonine-isoleucine polymorphism at residue 105, showing decreased activity and lower protein levels than the 105T protein. Molecular dynamic simulations at 37°C indicate that replacing Thr with the larger Ile residue leads to greater burial of residue 105 and heightened intramolecular interactions between residue 105 and residues within helix R3 and strand a3. This altered, tighter packing is translated to the active site, resulting in the reorientation of several cosubstrate-binding residues | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P50135 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| histamine N-methyltransferase | - |
Homo sapiens |
| HNMT | - |
Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
