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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

Renatured

Renatured on EC 2.7.3.3 - arginine kinase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
addition of 1% (v/v) Tween-20 and 0.6% (w/v) SDS to the dilution system leads to higher renaturation efficiency
after denaturation, the recombinant AK is successfully renatured and confirmed to be enzymatically active. Addition of Tween-20 and SDS to the dilution system lead to higher renaturation efficiency
in 0.2 mM KCl
-
reactivation of denatured enzyme AK: human cyclophilin A (CyPA) has a peptidyl-prolyl cis-trans isomerase (PPIase)-independent chaperone-like activity during enzyme AK folding. Recombinant rhCyPA can form dimers and trimers during the purification procedure, catalytically inactive recombinant cyclophilin A mutant variant Q63A has even more efficiency to suppress aggregation and improve reactivation yields of enzyme AK than the wild-type cyclophilin A, overview. Catalytically inactive cyclophilin A mutants R55A, F60A, and H126A can also act as chaperones in arginine kinase folding. The refolding is initiated by a 50fold dilution in 20 mM Tris-HCl buffer, pH 7.8, containing 10 mM 2-mercaptoethanol, in the presence or absence of 0.006 mM of the wild-type rhCyPA or its variants at 20°C
-
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course
-
the folding rate partly recovers to 60% as the inducing concentration of 1,1,1,3,3,3-hexafluoroisopropanol increases to 10% (v/v)
there are at least two intermediates in the refolding of urea-denatured dimeric arginine kinase. I1 (existing in 1.8-1.4 M urea) and I2 (existing in 0.8-0.4 M urea). I1 is a monomeric globular intermediate. I2 is an active native-like intermediate. The refolding of arginine kinase possesses a burst phase, fast phase and slow phase, which involves at least the burst phase intermediates
-