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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

Inhibitors

Inhibitors on EC 2.7.3.3 - arginine kinase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic acid
-
2-oxoglutarate
4-[[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl]-6,8-dimethyl-chromen-2-one
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis-(2-nitrobenzoic acid)
-
modification and inactivation course with DTNB and the reactivation course of DTNB-modified enzyme. Modified enzyme can be reactivated by an excess concentration of dithiothreitol in a monophasic kinetic course
5,5'-dithiobis-2-nitrobenzoic acid
-
-
5,7-dihydroxy-2-phenyl-6,8-bis(1-piperidylmethyl)chromen-4-one
Ag+
-
dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+
agmatine
aminoguanidine
-
10 mM, 2.6% inhibition
apoferritin
-
mixed inhibition
-
apoferritin-Ag nanoparticle
-
interaction with arginine kinase leads to more than 70% reduction in the enzyme activity, mixed inhibition
-
apoferritin-Au nanoparticle
-
interaction with arginine kinase leads to more than 70% reduction in the enzyme activity, mixed inhibition
-
apoferritin-Pt nanoparticle
-
interaction with arginine kinase leads to more than 70% reduction in the enzyme activity, mixed inhibition
-
aspartate
-
0.02-0.15 mM, causes inactivation and unfolding of arginine kinase
canavanine
chloride
citrulline
Creatine
D-Arg
D-arginine
-
competitive
D-glucose
the enzyme is inhibited by 50 mM D-glucose, almost all arginine kinase activity is lost after treatment with 200 mM D-glucose
dithiothreitol
-
conformational change and inactivation
DTNB
-
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course. This reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site
Ethylguanidine
5fold higher concentration than L-Arg, 22% inhibition
glutamate
glycine
guanidine
guanidine butyrate
-
10 mM, 4.3% inhibition
guanidine hydrochloride
His
5fold higher concentration than L-Arg, 50% inhibition
homoarginine
-
10 mM, 38.2% inhibition
Iodide
iodoacetamide
-
-
isoleucine
K+
-
200 mM, 50% inhibition
L-arginine
L-arginine methyl ester
-
competitive to L-Arg
L-Asp
5fold higher concentration than L-Arg, 25% inhibition
L-canavanine
L-Glu
5fold higher concentration than L-Arg, 31% inhibition
L-Glucose
AK-1 activity does not show significant variation after supplementation with 10 mM L-glucose. However, AK-1 activity decreases significantly when L-glucose concentration is higher than 50 mM and almost all MrAK-1 activity is lost after treatment with 200 mM L-glucose
L-histidine
-
10 mM, 2.4% inhibition
L-homoarginine
5fold higher concentration than L-Arg, 33% inhibition
L-Lys
5fold higher concentration than L-Arg, 25% inhibition
L-nitroarginine
lysine
Mg2+
-
at high concentrations noncompetitive inhibition of MgATP2-
MgADP-
-
inhibition is potentiated by NO3-
MgATP2-
-
enzyme form AK2 is strongly inhibited at high concentrations
Mn2+
-
at high concentrations noncompetitive inhibition of MgATP2-
N-methyl-L-Arg
5fold higher concentration than L-Arg, 28% inhibition
N-[2-(1H-imidazol-4-yl)ethyl]-3-[1-(2-methoxyethyl)indol-3-yl]propanamide
Na+
-
200 mM, 50% inhibition
NADH
-
noncompetitive
NH4+
-
200 mM, 50% inhibition
nitrate
nitrite
nitroarginine
ornithine
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal
putrescine
rutin
SDS
complete inactivation at 1.0 mM, the inactivation is a first-order reaction, with the kinetic processes shifting from a monophase to biphase as SDS concentrations increase. SDS concentrations lower than 5 mM do not induce conspicuous changes in tertiary structures, while higher concentrations of SDS exposedhydrophobic surfaces and induce conformational changes
thiocyanate
additional information
-