Crystallization (Comment) | Organism |
---|---|
purified arginine kinase in binary complex with arginine and in a ternary transition state analogue complex, mixing of 20 mg/ml protein in 10 mM Tris-HCl, pH 8.0, and 1 mM DTT, with with 4 mM L-arginine, 0.001 ml of the solution is then mixed with 0.001 ml of crystallization solution containing 0.2 M sodium acetate, 0.1 M sodium cacodylate, pH 6.5, and 30% w/v PEG 8000, 16°C, 3 weeks. For the ternary complex, the enzyme is cocrystallized with ADP 16 mM, MgCl2 20 mM, L-arginine 40 mM, and NaNO3 75 mM, X-ray diffraction structure determination and analysis at 1.6-1.9 A resolution | Penaeus vannamei |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Penaeus vannamei |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
x * 40000, about, SDS-PAGE | Penaeus vannamei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-arginine | Penaeus vannamei | - |
ADP + Nomega-phospho-L-arginine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Penaeus vannamei | Q004B5 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from abdominal muscles | Penaeus vannamei |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | abdominal muscle | Penaeus vannamei | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-arginine | - |
Penaeus vannamei | ADP + Nomega-phospho-L-arginine | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 40000, about, SDS-PAGE | Penaeus vannamei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Penaeus vannamei | |
ATP | - |
Penaeus vannamei |
General Information | Comment | Organism |
---|---|---|
additional information | the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, does not interact with arginine in the binary complex. Residue Glu324 is located in the flexible loop 310-320 that covers the active site and only stabilizes in the ternary transition state analogue complex, LvAK-TSAC | Penaeus vannamei |
physiological function | arginine kinase is a key enzyme for energetic balance in invertebrates and plays an important role in invertebrate physiology by buffering the ATP pool accordingly to cellular energy requirements | Penaeus vannamei |