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2.7.3.3: arginine kinase

This is an abbreviated version!
For detailed information about arginine kinase, go to the full flat file.

Word Map on EC 2.7.3.3

Reaction

ATP
+
L-arginine
=
ADP
+
Nomega-phospho-L-arginine

Synonyms

adenosine 5'-triphosphate-arginine phosphotransferase, adenosine 5'-triphosphate: L-arginine phosphotransferase, AK, AK-1, AK1, AK2, AK3, AK4, AK: L-arginine phosphotransferase, arginine kinase 1, arginine kinase 2, arginine kinase-1, arginine phosphokinase, ArgK, ARGK-2, ark, ATP: arginine N-phosphotransferase, ATP: arginine phosphotransferase, ATP: L-arginine phosphototransferase, ATP: L-arginine phosphotransferase, ATP:arginine N-phosphotransferase, ATP:arginine phosphotransferase, ATP:L-arginine N-phosphotransferase, ATP:L-arginine omega-N-phosphotransferase, ATP:L-arginine phosphotransferase, ESAK, F32B5.1, F44G3.2, F46H5.3, kinase, arginine (phosphorylating), McsB, MnAK2, MXAN2252 protein, PyAK1, PyAK2, PyAK3, PyAK4, rDer p 20, Tb09.160.4560, Tb927.9.6170, TbAK2, TbAK3, TcAK, TcAK1, TcAK2, W10C8.5, ZC434.8

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.3 Phosphotransferases with a nitrogenous group as acceptor
                2.7.3.3 arginine kinase

pH Stability

pH Stability on EC 2.7.3.3 - arginine kinase

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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 11
-
at pH 10.0, the relative activity is slightly reduced, in the pH range of 10–10.5, the relative activity decreases by almost 60% and above pH 11.0 the enzyme fully loses activity
674038
11 - 13
-
pH 11.0 is required to cause the complete loss of AK activity of the alkaline unfolded enzyme, the high pH denatured enzyme has some residual secondary and tertiary structure even at pH 13
674038
4 - 8
crayfish arginine kinase is stable at pH 4.0-8.0
738275
5.1
-
25°C, 15 min, 70% loss of activity
642456
5.4
-
25°C, 15 min, 20% loss of activity
642456
6 - 9.1
-
25°C, 15 min, stable
642456
8.5
-
30°C, 3 h, stable
642456
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
722436