Any feedback?
Literature summary for 2.7.3.3 extracted from
- Insight into structural aspects of histidine 284 of Daphnia magna arginine kinase (2020), Mol. Cells, 43, 784-792 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Daphnia magna |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop vapor diffusion method at 20°C. The crystal structure of H284A displays several structural changes, including the alteration of D324, a hydrogen-bonding network around H284, and the disruption of pi-stacking between the imidazole group of the H284 residue and the adenine ring of ATP | Daphnia magna |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H284A | the catalytic activity is reduced significantly compared to that in wild type enzyme. The crystal structure of H284A displays several structural changes, including the alteration of D324, a hydrogen-bonding network around H284, and the disruption of pi-stacking between the imidazole group of the H284 residue and the adenine ring of ATP | Daphnia magna |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.3 | - |
ATP | mutant enzyme H284A, pH and temperature not specified in the publication | Daphnia magna |  |
| 0.47 | - |
ATP | wild-type enzyme, pH and temperature not specified in the publication | Daphnia magna | |
| 0.9 | - |
L-arginine | wild-type enzyme, pH and temperature not specified in the publication | Daphnia magna | |
| 0.9 | - |
L-arginine | mutant enzyme H284A, pH and temperature not specified in the publication | Daphnia magna | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41000 | - |
SDS-PAGE | Daphnia magna |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-arginine | Daphnia magna | - |
ADP + Nomega-phospho-L-arginine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Daphnia magna | A0A0A7CK57 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Daphnia magna |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-arginine | - |
Daphnia magna | ADP + Nomega-phospho-L-arginine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 41000, SDS-PAGE | Daphnia magna |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
- |
Daphnia magna |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.19 | - |
ATP | mutant enzyme H284A, pH and temperature not specified in the publication | Daphnia magna | |
| 0.19 | - |
L-arginine | mutant enzyme H284A, pH and temperature not specified in the publication | Daphnia magna | |
| 18.6 | - |
ATP | wild-type enzyme, pH and temperature not specified in the publication | Daphnia magna | |
| 18.6 | - |
L-arginine | wild-type enzyme, pH and temperature not specified in the publication | Daphnia magna | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | 9.5 | - |
Daphnia magna |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 10 | pH 8.0: about 60% of maximal activity, pH 10.0: about 70% of maximal activity | Daphnia magna |
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
