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Literature summary for 2.7.3.3 extracted from

  • Shen, H.W.; Cao, M.J.; Cai, Q.F.; Ruan, M.M.; Mao, H.Y.; Su, W.J.; Liu, G.M.
    Purification, cloning, and immunological characterization of arginine kinase, a novel allergen of Octopus fangsiao (2012), J. Agric. Food Chem., 60, 2190-2199.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
x * 38000, SDS-PAGE Amphioctopus fangsiao

Organism

Organism UniProt Comment Textmining
Amphioctopus fangsiao
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephacryl S-200 gel filtration Amphioctopus fangsiao

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Amphioctopus fangsiao
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Amphioctopus fangsiao ADP + Nomega-phospho-L-Arg
-
r

Subunits

Subunits Comment Organism
? x * 38000, SDS-PAGE Amphioctopus fangsiao

Synonyms

Synonyms Comment Organism
ATP:L-arginine phosphotransferase
-
Amphioctopus fangsiao

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 40 the enzyme is relatively stable below 30°C, but the original bands become faint and the bands of aggregated enzyme (above 70 kDa) appear when the temperature is above 40°C Amphioctopus fangsiao

pH Stability

pH Stability pH Stability Maximum Comment Organism
9 10 the enzyme displays no obvious change when the pH value is below 9.0, but the original band of the enzyme is faint and the degraded fragments of the enzyme are observed when it is incubated at pH 9.5 and 10.0 for 1 h Amphioctopus fangsiao