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Literature summary for 2.7.3.3 extracted from

  • Suzuki, T.; Soga, S.; Inoue, M.; Uda, K.
    Characterization and origin of bacterial arginine kinases (2013), Int. J. Biol. Macromol., 57, 273-277.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene YH65_02995, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Sulfurovum lithotrophicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics, overview Sulfurovum lithotrophicum
0.071
-
ATP pH 8.0, 30°C, recombinant wild-type enzyme Sulfurovum lithotrophicum
0.401
-
L-arginine pH 8.0, 25°C, recombinant wild-type enzyme Sulfurovum lithotrophicum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Sulfurovum lithotrophicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-arginine Sulfurovum lithotrophicum
-
ADP + Nomega-phospho-L-arginine
-
r

Organism

Organism UniProt Comment Textmining
Sulfurovum lithotrophicum
-
gene YH65_02995
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme in Escherichia coli strain BL21(DE3) by metal affinity chromatography Sulfurovum lithotrophicum

Reaction

Reaction Comment Organism Reaction ID
ATP + L-arginine = ADP + Nomega-phospho-L-arginine random-order, rapid-equilibrium kinetic mechanism Sulfurovum lithotrophicum

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More the enzyme sequence is structurally divided into two domains, N- and C-terminal domains Sulfurovum lithotrophicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Sulfurovum lithotrophicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
88
-
L-arginine pH 8.0, 25°C, recombinant wild-type enzyme Sulfurovum lithotrophicum
88
-
ATP pH 8.0, 30°C, recombinant wild-type enzyme Sulfurovum lithotrophicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Sulfurovum lithotrophicum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Sulfurovum lithotrophicum

General Information

General Information Comment Organism
evolution the enzyme is widely distributed in invertebrate animals. The enzyme is also found in unicellular organisms, protists and bacteria, but its occurrence is intermittent among species. Detailed phylogenetic analysis, overview Sulfurovum lithotrophicum
physiological function arginine kinase plays a key role in ATP buffering systems of tissues and nerves that display high and variable rates of ATP turnover Sulfurovum lithotrophicum