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Literature summary for 2.7.3.3 extracted from

  • Lopez-Zavala, A.A.; Garcia-Orozco, K.D.; Carrasco-Miranda, J.S.; Sugich-Miranda, R.; Velazquez-Contreras, E.F.; Criscitiello, M.F.; Brieba, L.G.; Rudino-Pinera, E.; Sotelo-Mundo, R.R.
    Crystal structure of shrimp arginine kinase in binary complex with arginine-a molecular view of the phosphagen precursor binding to the enzyme (2013), J. Bioenerg. Biomembr., 45, 511-518.
    View publication on PubMed

Crystallization (Commentary)

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

Metals/Ions Comment Organism Structure
Mg2+ required Penaeus vannamei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
x * 40000, about, SDS-PAGE Penaeus vannamei

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Penaeus vannamei Q004B5
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from abdominal muscles Penaeus vannamei

Source Tissue

Source Tissue Comment Organism Textmining
muscle abdominal muscle Penaeus vannamei
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine
-
Penaeus vannamei ADP + Nomega-phospho-L-arginine
-
r

Subunits

Subunits Comment Organism
? x * 40000, about, SDS-PAGE Penaeus vannamei

Cofactor

Cofactor Comment Organism Structure
ADP
-
Penaeus vannamei
ATP
-
Penaeus vannamei

General Information

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