Any feedback?
Literature summary extracted from
- Ca2+-CaM activation of AMP deaminase contributes to adenine nucleotide dysregulation and phosphatidylserine externalization in human sickle erythrocytes (2009), Br. J. Haematol., 144, 434-445.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.4.6 | Calmodulin | Ca2+-calmodulin activates erythrocyte AMPD in conditions of disturbed calcium homeostasis during sickle cell disease | Homo sapiens |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.4.6 | Homo sapiens | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.5.4.6 | erythrocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.4.6 | AMP + H2O | - |
Homo sapiens | IMP + NH3 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.4.6 | 5'-adenosine monophosphate deaminase | - |
Homo sapiens |
| 3.5.4.6 | AMP deaminase | - |
Homo sapiens |
| 3.5.4.6 | AmpD | - |
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
