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ADP + Nomega-phospho-L-Arg
ATP + L-Arg
-
-
-
r
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
ADP + omega-N-phospho-L-Arg
ATP + L-arginine
function: five residues predicted to interact with the substrate arginine (S77, Y82, E239, C285 and E328), and five residues predicted to interact with the substrate ADP (R138, R140, R243, R294 and R323). Arginine (or phosphagen) and MgATP (or MgADP), typically exhibit synergistic binding to arginine kinase
-
-
r
ATP + 4-guanidinebutanoic acid
ADP + N-phospho-4-guanidinobutanoic acid
-
8% of the activity with L-Arg
-
-
?
ATP + 5-guanidinopentanoic acid
ADP + N-phospho-5-guanidinopentanoic acid
-
10% of the activity with L-Arg
-
-
?
ATP + CtsR-L-Arg
ADP + CtsR-N-phospho-L-Arg
-
McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes, phosphorylation of CtsR by McsB is sufficient to inhibit the repressor function of CtsR
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
ATP + L-arginine ethyl ester
ADP + Nomega-phospho-L-Arg ethyl ester
6% activity compared to L-Arg
-
-
?
ATP + L-arginine methyl ester
ADP + Nomega-phospho-L-arginine methyl ester
-
-
-
-
?
ATP + L-arginine-O-ethyl ester
?
-
isoform arginine kinase 2 shows about 16% activity of that obtained with L-Arg
-
-
?
ATP + L-argininic acid
ADP + Nomega-phospho-L-argininic acid
-
45% of the activity with L-Arg
-
-
?
ATP + L-canavanine
?
about 16% activity compared to L-Arg
-
-
?
ATP + L-canavanine
ADP + ?
arginine kinase TcAK1 shows approximately 15% reaction rate compared to L-arginine
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
ATP + L-Nalpha-acetylarginine
ADP + ?
arginine kinase TcAK1 shows approximately 15% reaction rate compared to L-arginine
-
-
?
ATP + lombricine
ADP + omega-N-phospholombricine
ATP + N-acetyl-L-Arg
ADP + Nomega-phospho-N-alpha-acetyl-L-Arg
-
13% of the activity with L-Arg
-
-
?
ATP + octopine
ADP + N-phospho-D-octopine
-
30% of the activity with L-Arg
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
GDP + Nomega-phospho-L-Arg
GTP + L-Arg
-
10% of the activity with ADP
-
-
?
GTP + L-arginine
GDP + Nomega-phospho-L-arginine
UDP + Nomega-phospho-L-Arg
UTP + L-Arg
-
10% of the activity with ADP
-
-
?
additional information
?
-
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
the enzyme is an important component of the energy releasing mechanism in the visual system that has high and fluctuating energy demands
-
-
?
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
-
the enzyme is a modulator of energetic reserves under starvation stress conditions, activity is post-transcriptionally regulated
-
-
?
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
-
-
-
-
?
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
-
-
-
-
r
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
-
-
-
-
r
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
-
-
-
r
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
-
-
-
r
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
no activity
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
no activity
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
D-Arg is phosphorylated to a lesser degree
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
D-Arg is as active as L-Arg
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
35.2% relative activity compared to L-Arg
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
35.2% of the activity with L-Arg
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
isoform AK1 shows 7.6% activity with D-arginine compared to L-arginine, isoform AK2 shows 35% activity with D-arginine compared to L-arginine
-
-
?
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
-
-
-
?
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
7.6% of the activity with L-Arg
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
McsB acts exclusively on L-Arg residues
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
highest activity
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
Isostychopus badonotus
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
the enzyme is stereospecific for the L-form over the D-form of its specific substrate arginine
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
production of high-energy reserves N-phospho-L-Arg in insect muscles
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
the enzyme is involved in the storage of the high-energy phosphate reserve phosphoarginine
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
strictly specific for ATP
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
100% activity
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
isoforms AK1 and AK2 are primarily active towards L-arginine
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
-
synergism in substrate binding
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
arginine kinase is an allergenic protein
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
synergism for substrate binding
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
specific reversible transfer of phosphate
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
the enzyme is specific for L-arginine. The activities for D-arginine, creatine, glycocyamine and taurocyamine are less than 1% that for l-arginine
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
the enzyme is highly stereo specific for L-arginine versus D-arginine
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
the enzyme is highly specific for L-arginine, reversible transfer of phosphate
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
enzymatic activity of arginine kinase AK4 is less by 3% than that of arginine kinase AK3
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
arginine kinase TcAK1 shows marked preference for L-arginine over D-arginine
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
arginine kinase TcAK2 shows marked preferences for L-arginine over D-arginine. Arginine kinase TcAK2 shows no activity with L-Nalpha-acetylarginine and L-canavanine
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
Crassostrea sp.
-
key enzyme in invertebrate energy metabolism
-
-
?
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
Pleocyemata sp.
-
-
-
-
?
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
both domains of Calyptogena arginine kinase are catalytically competent, although domain 2 strongly influences catalysis in domain 1
-
-
r
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
-
-
-
-
r
ATP + L-canavanine
ADP + L-phosphocanavanine
-
isoform arginine kinase 1 shows 10% activity of that obtained with L-Arg, isoform arginine kinase 2 shows about 9.5% activity of that obtained with L-Arg
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
-
-
-
r
ATP + L-canavanine
ADP + L-phosphocanavanine
-
L-canavanine is a weak substrate
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
-
7% of the activity with L-Arg
-
-
r
ATP + L-canavanine
ADP + L-phosphocanavanine
-
7.3% of the activity with L-Arg
-
-
r
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
-
isoform arginine kinase 2 shows about 37% activity of that obtained with L-Arg
-
-
?
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
7% activity compared to L-Arg
-
-
?
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
-
25% of the activity with L-Arg
-
-
?
ATP + lombricine
ADP + omega-N-phospholombricine
0.17% of the activity with L-Arg
-
-
?
ATP + lombricine
ADP + omega-N-phospholombricine
3.0% of the activity with L-Arg
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
0.11% of the activity with L-Arg
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
2.7% of the activity with L-Arg
-
-
?
GTP + L-arginine
GDP + Nomega-phospho-L-arginine
GTP shows 11% of the activity with ATP
-
-
r
GTP + L-arginine
GDP + Nomega-phospho-L-arginine
GTP shows 7% of the activity with ATP
-
-
r
additional information
?
-
no activity towards D-arginine, creatine, glycocyamine, and taurocyamine
-
-
?
additional information
?
-
-
no activity towards D-arginine, creatine, glycocyamine, and taurocyamine
-
-
?
additional information
?
-
-
L-arginine-O-ethyl ester and L-homo-arginine are extremely poor substrates for isoform AK1 with only 3.5% and 2% of the L-arginine reaction rate. L-Nalpha-acetyl-arginine, agmatine, creatine, 4-guanidino butyric acid, N7-methyl-arginine and N7-nitro-arginine are no substrates for isoform AK1. Minor substrates for isoform AK2 are L-Nalpha-acetyl-arginine and 4-guanidino butyric acid with 1.5% and 1.9% of the L-arginine reaction rate, respectively. Agmatine, creatine, L-N7-methyl-arginine and L-N7-nitro-arginine are no substrates for isoform AK2
-
-
?
additional information
?
-
arginine kinase exhibits no detectable activity towards L-ornithine, L-citrulline, or imino-L-ornithine, and only trace activity towards D-arginine
-
-
?
additional information
?
-
-
arginine kinase exhibits no detectable activity towards L-ornithine, L-citrulline, or imino-L-ornithine, and only trace activity towards D-arginine
-
-
?
additional information
?
-
no activity with D-arginine, N-acetyl-L-arginine, agmatine, and creatine
-
-
?
additional information
?
-
-
strictly specific for ATP
-
-
?
additional information
?
-
very little activity for 9.5 mM D-arginine and no activity for creatine, glycocyamine, and taurocyamine substrates examined at the final substrate concentration of 2.38 mM
-
-
?
additional information
?
-
-
very little activity for 9.5 mM D-arginine and no activity for creatine, glycocyamine, and taurocyamine substrates examined at the final substrate concentration of 2.38 mM
-
-
?
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(2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic acid
-
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+
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
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
guanidine butyrate
-
10 mM, 4.3% inhibition
His
5fold higher concentration than L-Arg, 50% inhibition
homoarginine
-
10 mM, 38.2% inhibition
K+
-
200 mM, 50% inhibition
L-arginine methyl ester
-
competitive to L-Arg
L-Asp
5fold higher concentration than L-Arg, 25% inhibition
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
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
NH4+
-
200 mM, 50% inhibition
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal
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
(2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic acid
ZINC12654467, probably competitive inhibitor identified by in silico screening
-
(2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic acid
-
ZINC12654467, probably competitive inhibitor identified by in silico screening
-
(2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic acid
-
ZINC12654467, probably competitive inhibitor identified by in silico screening
-
2-oxoglutarate
the enzyme activity is inhibited at 10-200 mM
2-oxoglutarate
the enzyme activity is inhibited by 10 mM 2-oxoglutarate
4-[[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl]-6,8-dimethyl-chromen-2-one
ZINC20412486, probably competitive inhibitor identified by in silico screening
4-[[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl]-6,8-dimethyl-chromen-2-one
-
ZINC20412486, probably competitive inhibitor identified by in silico screening
4-[[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl]-6,8-dimethyl-chromen-2-one
-
ZINC20412486, probably competitive inhibitor identified by in silico screening
5,7-dihydroxy-2-phenyl-6,8-bis(1-piperidylmethyl)chromen-4-one
i.e. ZINC08836734, probably competitive inhibitor identified by in silico screening
5,7-dihydroxy-2-phenyl-6,8-bis(1-piperidylmethyl)chromen-4-one
-
i.e. ZINC08836734, probably competitive inhibitor identified by in silico screening
5,7-dihydroxy-2-phenyl-6,8-bis(1-piperidylmethyl)chromen-4-one
-
i.e. ZINC08836734, probably competitive inhibitor identified by in silico screening
agmatine
65% inhibition at 2 mM
agmatine
61% enzyme inhibition at 2 mM
agmatine
5fold higher concentration than L-Arg, 20% inhibition
agmatine
-
10 mM, 79.3% inhibition
ATP
-
product inhibition, competitive with ADP, noncompetitive with L-Arg
ATP
the enzyme activity is inhibited at 100 mM
ATP
the enzyme is inhibited by 200 mM ATP
canavanine
81% inhibition at 2 mM
canavanine
79% enzyme inhibition at 2 mM
canavanine
5fold higher concentration than L-Arg, 50% inhibition
canavanine
-
10 mM, 54.6% inhibition
chloride
Isostychopus badonotus
-
9% inhibition at 50 mM
chloride
-
7% inhibition at 50 mM
chloride
-
50 mM, 7% inhibition
citrulline
17% inhibition at 2 mM
citrulline
21% enzyme inhibition at 2 mM
Creatine
11% inhibition at 2 mM
Creatine
9% enzyme inhibition at 2 mM
Creatine
-
10 mM, 12.7% inhibition
Cu2+
-
strong inhibition
D-Arg
-
product inhibition, competitive with arginine phosphate and noncompetitive withg ADP
D-Arg
-
competitive to L-arginine
glutamate
15% inhibition at 2 mM
glutamate
21% enzyme inhibition at 2 mM
glycine
10% inhibition at 2 mM
glycine
15% enzyme inhibition at 2 mM
guanidine
10% inhibition at 2 mM
guanidine
12% enzyme inhibition at 2 mM
guanidine hydrochloride
-
0.2 mM, about 90% loss of activity
guanidine hydrochloride
-
1 mM
Iodide
Isostychopus badonotus
-
13% inhibition at 50 mM
Iodide
-
3% inhibition at 50 mM
Iodide
-
50 mM, 3% inhibition
isoleucine
10% inhibition at 2 mM
isoleucine
9% enzyme inhibition at 2 mM
L-arginine
-
L-arginine
-
arginine kinase AK3 shows substrate inhibition. Residue S79 is essential for this phenomenon
L-arginine
-
after primary arginine substrate binding (ES complex formation), the binding of another arginine at the secondarily induced inhibitory site is accelerated to form the SES complex, causing substrate inhibition. S79 and V81 in the Paramecium AK3 are the key residues involved in substrate inhibition
L-canavanine
-
competitive to L-Arg
L-nitroarginine
5fold higher concentration than L-Arg, 28% inhibition
L-nitroarginine
-
10 mM, 52.6% inhibition
lysine
31% inhibition at 2 mM
lysine
3% enzyme inhibition at 2 mM
N-[2-(1H-imidazol-4-yl)ethyl]-3-[1-(2-methoxyethyl)indol-3-yl]propanamide
i.e. ZINC79191494, probably competitive inhibitor identified by in silico screening
N-[2-(1H-imidazol-4-yl)ethyl]-3-[1-(2-methoxyethyl)indol-3-yl]propanamide
-
i.e. ZINC79191494, probably competitive inhibitor identified by in silico screening
N-[2-(1H-imidazol-4-yl)ethyl]-3-[1-(2-methoxyethyl)indol-3-yl]propanamide
-
i.e. ZINC79191494, probably competitive inhibitor identified by in silico screening
nitrate
Isostychopus badonotus
-
88% inhibition at 50 mM
nitrate
-
99% inhibition at 50 mM
nitrate
-
50 mM, 99% inhibition
nitrite
Isostychopus badonotus
-
76% inhibition at 50 mM
nitrite
-
96% inhibition at 50 mM
nitrite
-
50 mM, 96% inhibition
nitroarginine
30% inhibition at 2 mM
nitroarginine
30% enzyme inhibition at 2 mM
ornithine
27% inhibition at 2 mM
ornithine
31% enzyme inhibition at 2 mM
putrescine
15% inhibition at 2 mM
putrescine
10% enzyme inhibition at 2 mM
rutin
-
-
rutin
-
noncompetitive inhibitor, i.e. 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxymethyl]oxan-2-yl]oxychromen-4-one, about 20% residual activity at 0.02-0.06 mM rutin
thiocyanate
Isostychopus badonotus
-
16% inhibition at 50 mM
thiocyanate
-
21% inhibition at 50 mM
thiocyanate
-
50 mM, 21% inhibition
Urea
10% inhibition at 2 mM
Urea
13% enzyme inhibition at 2 mM
Zn2+
-
strong inhibition
additional information
arginine kinase activity does not show significant variation after incubated with 10-200 mM L-citrulline, L-ornaline, and glycerol
-
additional information
-
arginine kinase activity does not show significant variation after incubated with 10-200 mM L-citrulline, L-ornaline, and glycerol
-
additional information
-
not inhibited by 50 mM acetate
-
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15
5-guanidinopentanoic acid
-
pH 8.5, 25°C
2.796
L-arginine ethyl ester
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
18
L-argininic acid
-
pH 8.5, 25°C
27
L-phosphocanavanine
-
37°C
0.63 - 1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
0.7 - 3.5
Nomega-phospho-L-Arg
1.4 - 14
Nomega-phospho-L-arginine
15
octopine
-
pH 8.5, 25°C
0.192
omega-N-phospho-L-arginine
-
-
additional information
additional information
-
0.0134
ADP
-
-
0.08
ADP
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
0.09
ADP
-
ADP in form of MgADP-
0.14
ADP
-
mutant enzyme E314Q
0.16
ADP
-
mutant enzyme E225Q
0.16
ADP
-
mutant enzyme E225Q/E314Q
0.16
ADP
-
mutant enzyme E314S
0.23
ADP
-
wild-type enzyme
0.26
ADP
-
mutant enzyme E225D
0.284
ADP
-
isoform arginine kinase 2
0.45
ADP
-
ADP in form of MgADP-
0.7
ADP
-
isoform arginine kinase 1
0.005
ATP
-
pH 8.6, 30°C
0.023
ATP
pH 8.0, 25°C, recombinant enzyme
0.071
ATP
-
pH 8.0, 30°C, recombinant wild-type enzyme
0.14
ATP
-
ATP in form of MgATP2-
0.16
ATP
pH 8.0, 25°C, recombinant enzyme
0.23
ATP
pH 7.5, 28°C, recombinant isozyme AK1
0.278
ATP
pH 8.0, 25°C, recombinant enzyme
0.3
ATP
in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25°C
0.3
ATP
mutant enzyme H284A, pH and temperature not specified in the publication
0.32
ATP
pH 7.5, 37°C, recombinant isozyme AK1
0.33
ATP
-
pH 8.1, mutant enzyme W208A
0.337
ATP
pH 8.0, 15°C, recombinant enzyme
0.339
ATP
pH 8.0, 17.5°C, recombinant enzyme
0.34
ATP
pH 8.0, 17.5°C, recombinant enzyme
0.35
ATP
pH 8.0, 25°C, recombinant enzyme
0.376
ATP
pH 8.0, 25°C, recombinant enzyme
0.399
ATP
pH 8.0, 20°C, recombinant enzyme
0.4
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.405
ATP
pH 8.0, 22.5°C, recombinant enzyme
0.422
ATP
pH 8.0, 15°C, recombinant enzyme
0.454
ATP
pH 8.0, 30°C, recombinant enzyme
0.46
ATP
-
37°C, two-domain enzyme
0.465
ATP
pH 8.0, 20°C, recombinant enzyme
0.47
ATP
wild-type enzyme, pH and temperature not specified in the publication
0.48
ATP
-
pH 8.1, wild-type enzyme
0.49 - 2
ATP
mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.654
ATP
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.661
ATP
-
isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.73
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
0.73
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
0.744
ATP
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.766
ATP
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.774
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.8
ATP
pH 7.5, 30°C, recombinant His-tagged enzyme
0.814
ATP
-
wild-type enzyme
0.814
ATP
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.82
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G
0.823
ATP
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.837
ATP
-
isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.9
ATP
pH 7.5, 30°C, recombinant His-tagged enzyme
0.926
ATP
-
isoform AK2 mutant G54S, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.93
ATP
-
isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.95
ATP
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C
0.97
ATP
-
37°C, domain 2
0.97
ATP
Crassostrea sp.
-
pH 7.9, 25°C, wild-type enzyme
0.988
ATP
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C
1.04
ATP
-
wild type enzyme
1.099
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F
1.12
ATP
-
isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
1.13
ATP
-
wild type enzyme isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
1.132
ATP
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C
1.17
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
1.25
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
1.26
ATP
pH 8.0, 25°C, recombinant enzyme
1.27
ATP
pH 8.0, 30°C, recombinant wild-type enzyme
1.27
ATP
-
pH 8.6, 30°C, recombinant arginine kinase
1.27
ATP
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
1.27
ATP
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
1.28
ATP
pH 8.0, 30°C, recombinant mutant T273S
1.29
ATP
pH 8.0, 30°C, wild-type enzyme
1.29
ATP
-
pH 8.6, 30°C, native arginine kinase
1.29
ATP
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
1.29
ATP
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
1.3
ATP
-
ATP in form of MgATP2-
1.32
ATP
pH 8.0, 30°C, recombinant mutant T273D
1.321
ATP
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C
1.36
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D
1.36
ATP
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C
1.4
ATP
-
ATP in form of MgATP2-
1.42
ATP
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C
1.49
ATP
-
mutant enzyme F315Y
1.49
ATP
-
mutant enzyme S312R/F315H/V319E
1.59
ATP
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
1.631
ATP
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C
1.64
ATP
pH 8.0, 30°C, recombinant mutant T273A
1.65
ATP
-
pH 8.6, 30°C, mutant enzyme P272G
1.7
ATP
pH 8.0, 30°C, recombinant mutant T273G
1.93
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D/P272R
2.08
ATP
-
mutant enzyme F315H
2.17
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
2.33
ATP
purified recombinant enzyme
2.38
ATP
-
mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30°C
2.42
ATP
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C
2.54
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
2.76
ATP
-
mutant enzyme F315A
2.84
ATP
-
pH 8.6, 30°C, mutant enzyme P272R
2.99
ATP
-
wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.092
ATP
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C
3.49
ATP
-
isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.56
ATP
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30°C
3.68
ATP
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C
3.7 - 5
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
3.72
ATP
-
isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
4.06
ATP
-
mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30°C
4.15
ATP
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C
4.2
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F/P272G
13.3
ATP
-
mutant enzyme S282G
1.3
D-Arg
-
pH 8.5, 25°C
3.14
D-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
4.4
D-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
6.45
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
9
D-Arg
-
wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25°C
9.34
D-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C
9.55
D-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C
13.9
D-Arg
the reaction mixture contains 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate made up in 100 mM imidazole/HCl (pH 7), 5 mM NADH made up in Tris/HCl (pH 8), pyruvate kinase/lactate dehydrogenase mixture made up in 100 mM imidazole/HCl (pH 7), 100 mM ATP made up in 100 mM imidazole/HCl (pH 7), and recombinant enzyme, at 25°C
0.106
L-Arg
mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.12
L-Arg
in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25°C
0.126
L-Arg
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.15
L-Arg
-
pH 8.6, 25°C
0.18
L-Arg
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.21
L-Arg
-
isoform arginine kinase 2
0.211
L-Arg
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.26
L-Arg
-
37°C, domain 2
0.37
L-Arg
-
pH 7.5, 26°C
0.389
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.413
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.42
L-Arg
-
37°C, two-domain enzyme
0.421
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.52
L-Arg
-
wild type enzyme
0.52
L-Arg
-
37°C, D197G mutant enzyme of domain 2
0.578
L-Arg
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C
0.594
L-Arg
native enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
0.603
L-Arg
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
0.67
L-Arg
25°C, mutant enzyme D62G
0.68
L-Arg
25°C, recombinant wild-type enzyme
0.744
L-Arg
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C
0.84
L-Arg
-
mutant enzyme F315Y
0.91
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75D
0.94
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75F
0.94
L-Arg
-
pH 8.6, 30°C, native arginine kinase
0.94
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.94
L-Arg
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.95
L-Arg
-
pH 8.6, 30°C, recombinant arginine kinase
0.951
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.951
L-Arg
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.98
L-Arg
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C
0.99
L-Arg
-
mutant enzyme S312R/F315H/V319E
0.99
L-Arg
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C
1.01
L-Arg
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C
1.02
L-Arg
-
37°C, H60R mutant of domain 2
1.02
L-Arg
25°C, native enzyme
1.036
L-Arg
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C
1.13
L-Arg
-
mutant enzyme F315H
1.27
L-Arg
-
isoform arginine kinase 1
1.53
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75D/P272R
1.571
L-Arg
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C
1.74
L-Arg
25°C, native enzyme
1.74
L-Arg
-
mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30°C
1.81
L-Arg
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C
2.05
L-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C
2.5 - 3
L-Arg
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30°C
2.67
L-Arg
-
mutant enzyme F315A
2.72
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
2.726
L-Arg
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C
2.82
L-Arg
25°C, native enzyme
2.85
L-Arg
-
pH 8.6, 30°C, mutant enzyme P272R
2.98
L-Arg
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C
3.04
L-Arg
-
mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30°C
3.25
L-Arg
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C
3.45
L-Arg
25°C, mutant enzyme S63G
3.6
L-Arg
-
37°C, H60G mutant of domain 2
3.69
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.78
L-Arg
-
pH 8.6, 30°C, mutant enzyme P272G
3.98
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75F/P272G
4.2
L-Arg
the reaction mixture contains 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate made up in 100 mM imidazole/HCl (pH 7), 5 mM NADH made up in Tris/HCl (pH 8), pyruvate kinase/lactate dehydrogenase mixture made up in 100 mM imidazole/HCl (pH 7), 100 mM ATP made up in 100 mM imidazole/HCl (pH 7), and recombinant enzyme, at 25°C
5.07
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
6.45
L-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.014
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme Q80S
0.021
L-arginine
-
pH 8.6, 30°C
0.035
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme Q80A
0.054
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.065
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme D77A
0.076
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, wild-type enzyme
0.124
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme G298R
0.131
L-arginine
pH 8.0, 15°C, recombinant enzyme
0.165
L-arginine
pH 8.0, 20°C, recombinant enzyme
0.166
L-arginine
pH 8.0, 15°C, recombinant enzyme
0.179
L-arginine
pH 8.0, 17.5°C, recombinant enzyme
0.196
L-arginine
pH 8.0, 17.5°C, recombinant enzyme
0.24
L-arginine
pH 7.5, 28°C, recombinant isozyme AK1
0.26
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
0.284
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK4, mutant enzyme R298G
0.29
L-arginine
pH 8.0, 22.5°C, recombinant enzyme
0.3
L-arginine
pH 8.0, 20°C
0.3
L-arginine
pH 7.5, 30°C, recombinant His-tagged enzyme
0.302
L-arginine
pH 8.0, 20°C, recombinant enzyme
0.307
L-arginine
-
mutant enzyme Y89R
0.31
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
0.344
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.348
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme S79A
0.35
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G
0.35
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, wild-type enzyme
0.35
L-arginine
pH 7.5, 30°C, recombinant His-tagged enzyme
0.35
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
0.37
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.386
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK4, wild-type enzyme
0.401
L-arginine
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.41
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.413
L-arginine
-
wild-type enzyme
0.439
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.456
L-arginine
pH 8.0, 30°C, recombinant enzyme
0.48
L-arginine
pH 7.5, 37°C, recombinant isozyme AK1
0.538
L-arginine
pH 8.0, 30°C, recombinant enzyme
0.546
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme D78A
0.558
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme V81A
0.63
L-arginine
-
mutant enzyme H64G
0.66
L-arginine
-
pH 8.1, wild-type enzyme
0.7
L-arginine
-
pH 8.1, mutant enzyme W208A
0.779
L-arginine
pH 8.0, 35°C, recombinant enzyme
0.81
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
0.88
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.9
L-arginine
wild-type enzyme, pH and temperature not specified in the publication
0.9
L-arginine
mutant enzyme H284A, pH and temperature not specified in the publication
0.912
L-arginine
wild-type two-domain enzyme
0.94
L-arginine
pH 8.0, 30°C, wild-type enzyme
0.95
L-arginine
pH 8.0, 30°C, recombinant wild-type enzyme
0.965
L-arginine
-
mutant enzyme D62G
0.98
L-arginine
pH 8.0, 30°C, recombinant mutant T273S
1.04
L-arginine
pH 8.0, 30°C, recombinant mutant T273D
1.16
L-arginine
-
mutant enzyme S282G
1.196
L-arginine
-
mutant enzyme D62_F63delinsDGF
1.44
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
1.45
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
1.46
L-arginine
-
mutant enzyme R193G
1.5
L-arginine
pH 7.5, 30°C, arginine kinase TcAK1
1.57
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
1.7
L-arginine
pH 8.6, 30°C
1.79
L-arginine
pH 7.5, 30°C
3.05
L-arginine
pH 8.0, 30°C, recombinant mutant T273A
3.18
L-arginine
pH 8.0, 30°C, recombinant mutant T273G
3.7
L-arginine
pH 7.5, 30°C, arginine kinase TcAK2
8.458
L-arginine
-
mutant enzyme F63G
6.7
L-canavanine
-
-
0.63
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
wild-type enzyme
0.68
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314D
0.72
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225D
0.88
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q
0.92
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
0.94
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
-
0.98
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314S
1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q/E314Q
0.7
Nomega-phospho-L-Arg
-
37°C
0.73
Nomega-phospho-L-Arg
-
pH 7.5, 26°C
0.74
Nomega-phospho-L-Arg
-
isoform arginine kinase 2
1.166
Nomega-phospho-L-Arg
native enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
1.432
Nomega-phospho-L-Arg
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
2.08
Nomega-phospho-L-Arg
-
pH 6.7, 25°C
2.1
Nomega-phospho-L-Arg
at pH 8.0 and 25°C
2.31
Nomega-phospho-L-Arg
-
isoform arginine kinase 1
3.5
Nomega-phospho-L-Arg
-
pH 7.2, 25°C
1.4
Nomega-phospho-L-arginine
pH 7.5, 30°C, arginine kinase TcAK2
14
Nomega-phospho-L-arginine
pH 7.5, 30°C, arginine kinase TcAK1
additional information
additional information
-
-
-
additional information
additional information
Pleocyemata sp.
-
-
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
-
bisubstrate kinetics and binary dissociation constants, overview
-
additional information
additional information
determination of activation energy for transition state of AK reactions, thermodynamics
-
additional information
additional information
determination of activation energy for transition state of AK reactions, thermodynamics
-
additional information
additional information
dissociation consants of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetic analysis, overview. The enzyme shows a random-order, rapid equilibrium kinetic mechanism
-
additional information
additional information
Michaelis-Menten kinetic analysis, overview. The enzyme shows a random-order, rapid equilibrium kinetic mechanism
-
additional information
additional information
-
Michaelis-Menten kinetic analysis, overview. The enzyme shows a random-order, rapid equilibrium kinetic mechanism
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
-
steady-state kinetic analysis, sequential ternary kinetic model, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
27.3
L-(+)-(S)-canavanine
-
-
50.7
L-phosphocanavanine
-
-
0.27 - 140
N5-(N-phosphonocarbamimidoyl)-L-ornithine
0.093 - 431
Nomega-phospho-L-Arg
22 - 146.1
Nomega-phospho-L-arginine
1.11
omega-N-phospho-L-arginine
-
pH 8, 25°C
additional information
additional information
Pleocyemata sp.
-
-
-
0.27
ADP
-
mutant enzyme E225Q/E314Q
0.34
ADP
-
mutant enzyme E225D
0.37
ADP
-
mutant enzyme E314Q
0.45
ADP
-
mutant enzyme E225Q
2.17
ADP
-
mutant enzyme E314D
116
ADP
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
140
ADP
-
wild-type enzyme
0.00229
ATP
-
mutant enzyme L65G
0.005
ATP
-
mutant enzyme E314V
0.0329
ATP
-
mutant enzyme D62_F63delinsDGF
0.19
ATP
mutant enzyme H284A, pH and temperature not specified in the publication
0.443
ATP
-
mutant enzyme R193G
0.913
ATP
-
mutant enzyme D62G
3.31
ATP
-
mutant enzyme F63G
8.92
ATP
-
25°C, H60G mutant of domain 2
9.22
ATP
-
mutant enzyme Y89R
9.53
ATP
-
25°C, D197G mutant of domain 2
11.4
ATP
pH 8.0, 25°C, recombinant enzyme
18.09
ATP
-
mutant enzyme H64G
18.1
ATP
-
25°C, H60R mutant of domain 2
18.6
ATP
wild-type enzyme, pH and temperature not specified in the publication
22.8
ATP
-
mutant enzyme S282G
22.9
ATP
wild-type two-domain enzyme
24.4
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
25.3
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G
25.7
ATP
-
wild-type enzyme
32.4
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
33.4
ATP
-
isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
36.6
ATP
-
wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
38.9
ATP
-
pH 7.5, 25°C, recombinant enzyme
39.5
ATP
-
wild type isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
40
ATP
pH 8.0, 25°C, recombinant enzyme
40.8
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
41
ATP
-
isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
41.9
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
41.9
ATP
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
42.1
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
43.2
ATP
-
isoform AK2 mutant G54S, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
43.3
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
44.7
ATP
-
25°C, domain 2
45
ATP
pH 8.0, 25°C, recombinant enzyme
47.5
ATP
Crassostrea sp.
-
pH 7.9, 25°C, wild-type enzyme
50.1
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
54.16
ATP
pH 8.0, 30°C, recombinant mutant T273G
60.3
ATP
-
pH 8.6, 30°C, mutant enzyme P272R
60.7
ATP
-
isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
60.97
ATP
pH 8.0, 30°C, recombinant mutant T273A
61.8
ATP
-
isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
63.4
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
65.8
ATP
-
isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
68.3
ATP
-
isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
73.3
ATP
-
25°C, two-domain enzyme
74.6
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F/P272G
79.2
ATP
-
pH 8.6, 30°C, mutant enzyme P272G
88
ATP
-
pH 8.0, 30°C, recombinant wild-type enzyme
104
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
126.2
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F
129
ATP
recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains
140.7
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D
141.3
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D/P272R
143.2
ATP
pH 8.0, 30°C, recombinant mutant T273D
151.3
ATP
pH 8.0, 30°C, recombinant mutant T273S
159.4
ATP
pH 8.0, 30°C, recombinant wild-type enzyme
159.4
ATP
-
pH 8.6, 30°C, recombinant arginine kinase
163
ATP
pH 8.0, 30°C, wild-type enzyme
163
ATP
-
pH 8.6, 30°C, native arginine kinase
180
ATP
pH 8.0, 25°C, recombinant enzyme
2 - 3.7
D-Arg
the reaction mixture contains 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate made up in 100 mM imidazole/HCl (pH 7), 5 mM NADH made up in Tris/HCl (pH 8), pyruvate kinase/lactate dehydrogenase mixture made up in 100 mM imidazole/HCl (pH 7), 100 mM ATP made up in 100 mM imidazole/HCl (pH 7), and recombinant enzyme, at 25°C
40.8
D-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
61.5
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
86.7
D-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C
90.7
D-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
90.7
D-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C
121
D-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.08
L-Arg
-
mutant enzyme S312G/E314V/F315D/E317A/S318A/G321S
0.833
L-Arg
-
mutant enzyme F315Y
1.02
L-Arg
-
mutant enzyme F315A
1.1
L-Arg
-
wild type enzyme
2.02
L-Arg
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C
2.73
L-Arg
-
two-domain enzyme, in 100 mM Tris-HCl (pH 8.0), at 10°C
3.97
L-Arg
-
mutant enzyme F315H
4.3
L-Arg
-
two-domain enzyme, in 100 mM Tris-HCl (pH 8.0), at 25°C
4.38
L-Arg
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C
5.54
L-Arg
-
mutant enzyme S312R/F315H/V319E
7.4
L-Arg
-
isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 10°C
8.92
L-Arg
-
25°C, H60G mutant of domain 2
9.53
L-Arg
-
25°C, D197G mutant of domain 2
10.26
L-Arg
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C
13.09
L-Arg
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C
13.7
L-Arg
-
isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 25°C
15.67
L-Arg
-
mutant enzyme F315Y
15.95
L-Arg
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C
18.1
L-Arg
-
25°C, H60R mutant of domain 2
18.66
L-Arg
-
wild type enzyme
23.33
L-Arg
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C
25.7
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
29.93
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
34.8
L-Arg
mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
35.4
L-Arg
the reaction mixture contains 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate made up in 100 mM imidazole/HCl (pH 7), 5 mM NADH made up in Tris/HCl (pH 8), pyruvate kinase/lactate dehydrogenase mixture made up in 100 mM imidazole/HCl (pH 7), 100 mM ATP made up in 100 mM imidazole/HCl (pH 7), and recombinant enzyme, at 25°C
43.3
L-Arg
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
44.7
L-Arg
-
25°C, domain 2
45.1
L-Arg
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
45.9
L-Arg
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
46
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
56.21
L-Arg
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C
60.36
L-Arg
-
mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30°C
62.3
L-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C
64.43
L-Arg
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C
70.93
L-Arg
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30°C
73.3
L-Arg
-
25°C, two-domain enzyme
75.4
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
77.8
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
81
L-Arg
in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25°C
81.2
L-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C
89
L-Arg
-
mutant two-domain-enzyme D1(Y68G)-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C
104
L-Arg
-
wild type one-domain-enzyme D1, in 100 mM Tris/HCl, pH 8.0 at 25°C
105.6
L-Arg
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C
109.8
L-Arg
-
mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30°C
121
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
123
L-Arg
-
mutant two-domain-enzyme D1-D2(Y68G), in 100 mM Tris/HCl, pH 8.0 at 25°C
129
L-Arg
recombinant wild-type enzyme with MBP tag
151.2
L-Arg
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C
152.2
L-Arg
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C
157
L-Arg
-
wild type one-domain-enzyme D2, in 100 mM Tris/HCl, pH 8.0 at 25°C
159.4
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
159.4
L-Arg
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
163
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
163
L-Arg
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
187
L-Arg
-
mutant two-domain-enzyme D1-Lys6-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C
678
L-Arg
-
wild type two-domain-enzyme D1-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C
0.00229
L-arginine
-
mutant enzyme L65G
0.005
L-arginine
-
mutant enzyme E314V
0.0329
L-arginine
-
mutant enzyme D62_F63delinsDGF
0.19
L-arginine
mutant enzyme H284A, pH and temperature not specified in the publication
0.443
L-arginine
-
mutant enzyme R193G
0.913
L-arginine
-
mutant enzyme D62G
3.31
L-arginine
-
mutant enzyme F63G
6.74
L-arginine
pH 7.5, 30°C
9.22
L-arginine
-
mutant enzyme Y89R
11.4
L-arginine
pH 8.0, 25°C, recombinant enzyme
12.7
L-arginine
pH 7.5, 30°C, arginine kinase TcAK2
18.09
L-arginine
-
mutant enzyme H64G
18.6
L-arginine
wild-type enzyme, pH and temperature not specified in the publication
22.8
L-arginine
-
mutant enzyme S282G
24.4
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
25.3
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G
25.7
L-arginine
-
wild-type enzyme
32.4
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
38.9
L-arginine
-
pH 7.5, 25°C, recombinant enzyme
40
L-arginine
pH 8.0, 25°C, recombinant enzyme
40.8
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
41.9
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
42.1
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
45
L-arginine
pH 8.0, 25°C, recombinant enzyme
47.5
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, wild-type enzyme
54.16
L-arginine
pH 8.0, 30°C, recombinant mutant T273G
60.97
L-arginine
pH 8.0, 30°C, recombinant mutant T273A
63.4
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
75
L-arginine
pH 8.6, 30°C
84.8
L-arginine
pH 8.0, 20°C
88
L-arginine
-
pH 8.0, 25°C, recombinant wild-type enzyme
104
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
108
L-arginine
pH 8.0, 15°C, recombinant enzyme
134
L-arginine
pH 8.0, 17.5°C, recombinant enzyme
143.2
L-arginine
pH 8.0, 30°C, recombinant mutant T273D
151.3
L-arginine
pH 8.0, 30°C, recombinant mutant T273S
159.4
L-arginine
pH 8.0, 30°C, recombinant wild-type enzyme
163
L-arginine
pH 8.0, 30°C, wild-type enzyme
170
L-arginine
pH 8.0, 15°C, recombinant enzyme
172.7
L-arginine
pH 7.5, 30°C, arginine kinase TcAK1
174
L-arginine
pH 8.0, 20°C, recombinant enzyme
180
L-arginine
pH 8.0, 25°C, recombinant enzyme
183
L-arginine
pH 8.0, 17.5°C, recombinant enzyme
196
L-arginine
pH 8.0, 22.5°C, recombinant enzyme
212.9
L-arginine
wild-type two-domain enzyme
217
L-arginine
pH 8.0, 25°C, recombinant enzyme
244
L-arginine
pH 8.0, 20°C, recombinant enzyme
272
L-arginine
pH 8.0, 25°C, recombinant enzyme
343
L-arginine
pH 8.0, 30°C, recombinant enzyme
459
L-arginine
pH 8.0, 35°C, recombinant enzyme
0.27
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q/E314Q
0.34
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225D
0.37
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314D
0.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q
2.17
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314S
116
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
140
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
wild-type enzyme
0.093
Nomega-phospho-L-Arg
at pH 8.0 and 25°C
431
Nomega-phospho-L-Arg
-
-
22
Nomega-phospho-L-arginine
pH 7.5, 30°C, arginine kinase TcAK1
146.1
Nomega-phospho-L-arginine
pH 7.5, 30°C, arginine kinase TcAK2
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evolution
arginine kinase genes in trypanosomatids, phylogenetic analysis, overview
evolution
phosphoarginine and arginine kinase are the most commonly found phosphagen and phosphagen kinase in invertebrates, such as arthropods, marine invertebrates, Haemonchus contortus larvae, the entomopathogenic nematode Steinernema carpocapsae, and the protozoan parasite Trypanosoma cruzi
evolution
phosphoarginine and arginine kinase are the most commonly found phosphagen and phosphagen kinase in invertebrates, such as arthropods, marine invertebrates, Haemonchus contortus larvae, the entomopathogenic nematode Steinernema carpocapsae, and the protozoan parasite Trypanosoma cruzi
evolution
-
phylogenetic analysis of amino acid sequences of phosphagen kinases indicate that the Myzostoma AK gene lineage differs from that of the polychaete Sabellastarte spectabilis AK, which is a dimer of creatine kinase (CK) origin. It is likely that the Myzostoma AK gene lineage was lost at an early stage of annelid evolution and that Sabellastarte AK evolved secondarily from the CK gene. Analysis of evolution of phosphagen kinases of annelids with marked diversity, overview
evolution
the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.
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
evolution
-
the enzyme is widely distributed in various invertebrates and many lower chordates but absent in vertebrates
evolution
two putative AK genes in the genome of Tetrahymena thermophila: one is a typical AK with a 40-kDa subunit (AK1) and the other is an unusual two-domain AK2 having an 80-kDa contiguous dimer, which appears to be the result of gene duplication and subsequent fusion
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
two distinct arginine kinase gene lineages are present in cnidarians. Phylogenetic analysis suggestes that the Corallium rubrum arginine kinase sequence has a distinct origin from that of other known cnidarian arginine kinases with unusual two-domain structure
evolution
-
two distinct arginine kinase gene lineages are present in cnidarians. Phylogenetic analysis suggestes that the Corallium rubrum arginine kinase sequence has a distinct origin from that of other known cnidarian arginine kinases with unusual two-domain structure
malfunction
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
malfunction
-
larval settlement rate decreases and larval movement is inhibited in response to treatments with high concentrations of enzyme inhibitors rutin and quercetin
malfunction
RNAi knockdown of all three arginine kinase isozymes induces a growth defect that is more prominent when the cells are exposed to oxidative stress. Loss of flagellar isozyme AK1 reduces swim velocity without visible alteration of flagellar morphology. The absence of isozyme AK1 results in reduced infectivity by procyclic trypanosomes for tsetse flies
malfunction
-
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
-
malfunction
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
-
metabolism
-
arginine kinase mainly participates in energy metabolism in invertebrates. Arginine kinase is functionally analogous to creatine kinase, EC 2.7.3.2, in vertebrates
metabolism
the opposite hormonal regulation of arginine kinase TcAK1 and arginine kinase TcAK2 is mediated by transcription factor Broad-Complex
physiological function
arginine kinase may play an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
arginine kinase is involved in the antiviral process of Bombyx mori larvae against nucleopolyhedrovirus infection
physiological function
the enzyme plays an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
physiological function
arginine kinase is a key enzyme for cellular energy metabolism, catalyzing the reversible phosphoyl transfer from phosphoarginine to ADP in invertebrates
physiological function
arginine kinase is a key enzyme for energetic balance in invertebrates and plays an important role in invertebrate physiology by buffering the ATP pool accordingly to cellular energy requirements
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
physiological function
isozyme AK1 confers a competitive advantage in infections of tsetse flies in midgut by the parasite, overview
physiological function
isozyme AK1 plays a role in the phosphoarginine shuttle, which enables a continuous energy flow to dynein for ciliary movement in Tetrahymena pyriformis
physiological function
-
the enzyme is involved in the larval settlement through mediating energy supply in muscle tissues. The enzyme mainly provides energy for muscle movements and is essential for motility in arthropods
physiological function
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
physiological function
arginine kinase AK3 is likely to be located in theciliary membrane and influences swimming velocity, presumably through the phosphoarginine shuttle system present in cilia
physiological function
arginine kinase MnAK2 may play a crucial role in the response to salinity stress in Macrobrachium nipponense. Arginine kinase plays imperative roles in innate immune feedback and stress resistance in invertebrates
physiological function
arginine kinase plays a fundamental role in energy homeostasis. The enzyme interacts with the transmembrane protein 2MIT and is involved in Drosophila melanogaster short-term memory
physiological function
arginine kinase TcAK1 and arginine kinase TcAK2 play similar roles in adult fertility and stress response
physiological function
the enzyme has a regulatory role during larval settlement. It is involved in both locomotion and substratum exploration during larval settlement. Decreased arginine kinase activity in swimming larvae leads to inhibition of larval settlement
physiological function
the enzyme is an enzyme crucial for energy metabolism, keeping the pool of phosphagens in invertebrates, and also an allergen for humans
physiological function
-
the enzyme is involved in temporal and spatial ATP buffering systems. It plays an important role in physiological function and metabolic regulations, in particular tissues with high and fluctuating energy demands. Possible involvement of arginine kinases (PyAKs) in energetic homeostasis during environmental changes
physiological function
-
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
-
physiological function
-
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
-
additional information
-
enzyme structure homology modeling and docking simulations, overview
additional information
enzyme structure homology modelling, overview
additional information
isozyme AK1 has two insertions of respectively 22 and 26 amino acids at the N- and C-terminus
additional information
-
isozyme AK1 has two insertions of respectively 22 and 26 amino acids at the N- and C-terminus
additional information
residue C271 is involved in the enzyme activity and constraining the orientation of the substrate arginine. Residue T273 interacts with C271 and plays a vital role in the enzyme activity, substrate synergism, and structural stability
additional information
the active region of enzyme AK is more flexible than the overall enzyme molecule
additional information
-
the active region of enzyme AK is more flexible than the overall enzyme molecule
additional information
the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, does not interact with arginine in the binary complex. Residue Glu324 is located in the flexible loop 310-320 that covers the active site and only stabilizes in the ternary transition state analogue complex, LvAK-TSAC
additional information
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
-
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
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Y68A
introduction of a Y68A mutation in both domains virtually abolishes catalytic activity. Significant residual activity is observed, when the Y68A mutation is introduced only into domain 2 of the two-domain enzyme. A similar mutation in domain 1 of the two domain enzyme reduces activity to a much lower extent
D62E
introduction of Glu at position 62 in isolated domain 2. The catalytic efficiency of D2/D62E is similar to that of the two-domain wild-type enzyme. This replacement does not alter synergistic substrate binding relative to wild-type domain 2
D62G
introduction of Gly at position 62 in isolated domain 2. The catalytic efficiency of the D2/D62G mutant is decreased to 13% that of wild-type domain 2
Y68G
-
the mutation in domain 1 or 2 leads to almost no catalytic activity
D57A
-
the mutation causes pronounced loss of activity and substrate synergism, and distinct conformational changes
D57E
-
most of the kinetic parameters are similar to those of wild type enzyme. A small decrease in Kd/Km and kcat/Km (L-Arg) values indicate a slight loss of substrate synergism and catalytic efficiency
D62G
-
2.3fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 3.5% of the wild-type value
D62_F63delinsDGF
-
2.9fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 0.01% of the wild-type value
delN56_V58
-
inactive mutant enzyme
E314D
-
significantly decreased activity
E314Q
-
significantly decreased activity
F315A
-
modest AK activity
F315H
-
modest AK activity
F315Y
-
modest AK activity
F63G
-
20.48fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 12.9% of the wild-type value
H64G
-
1.53fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 70.4% of the wild-type value
L65G
-
turnover number is 0.0011% of the wild-type value
Q53A
-
the mutation causes pronounced loss of activity and substrate synergism, and distinct conformational changes
Q53A/D57A
-
the changes in kinetic parameters as well as the loss of substrate synergism of the double mutant are more severe than that of Q53A and D57A single mutant enzymes. In addition, the double mutant has the lowest affinity for ATP
Q53E
-
most of the kinetic parameters are similar to those of wild type enzyme. A small decrease in Kd/Km and kcat/Km (L-Arg) values indicate a slight loss of substrate synergism and catalytic efficiency
R193G
-
3.5fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 1.7% of the wild-type value
S282G
-
2.81fold increase in KM-value for L-arginine compared to wild-type value, 16.34fold increase in KM-value for ATP compared to wild-type value, turnover number is 88.7% of the wild-type value
S312G/E314V/F315D/E317A/S318A/G321S
-
slight arginine kinase activity
S312R/F315H/V319E
-
modest AK activity
W208A
-
mutant enzyme shows 70.3% of the wild-type enzyme in the forward reaction. Mutation makes the enzyme susceptible to heat and denaturants, sich as guanidine HCl
W218A
-
mutation causes almost complete loss of activity and decreases the melting temperature in differential scanning calometry profiles and decreases stability against guanidine hydrochloride denaturation
Y89R
-
1.35fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 35.9% of the wild-type value
A105S
the mutant shows decreased Km values and turnover number for L-Arg (about 120% affinity) and ATP as well as slightly decreased catalytic efficiency (to about 90%) compared to the wild type enzyme
A105S/S106G
the mutant shows increased Km values and turnover number for L-Arg (about 70% affinity) and ATP as well as decreased catalytic efficiency (to about 70%) compared to the wild type enzyme
S106G
the mutant shows increased Km values and turnover number for L-Arg (about 60% affinity) and ATP as well as decreased catalytic efficiency (to about 60%) compared to the wild type enzyme
D197G
-
mutant of domain 2, affinity for Arg in mutant enzyme is reduced considerably, accompanied by a decrease in Vmax
H60G
-
mutant of domain 2, affinity for Arg in mutant enzyme is reduced considerably, accompanied by a decrease in Vmax
H60R
-
mutant of domain 2, affinity for Arg in mutant enzyme is reduced considerably, accompanied by a decrease in Vmax
K193G
Crassostrea sp.
-
turnover number is 68% of the wild-type value, KM-value for L-arginine is 4.1fold higher than wild-type value, Km-value for ATP is 2.2fold higher than wild-type value
K194R
Crassostrea sp.
-
turnover number is 85% of the wild-type value, KM-value for L-arginine is 4.5fold higher than wild-type value, Km-value for ATP is 1.3fold higher than wild-type value
N62D
Crassostrea sp.
-
turnover number is 88% of the wild-type value, KM-value for L-arginine is 1.1fold lower than wild-type value, Km-value for ATP is 1.2fold higher than wild-type value
N62D/K193R
Crassostrea sp.
-
turnover number is 89% of the wild-type value, KM-value for L-arginine is 2.3fold higher than wild-type value, Km-value for ATP is 1.6fold higher than wild-type value
N62G
Crassostrea sp.
-
turnover number is 53% of the wild-type value, KM-value for L-arginine is identical to wild-type value, Km-value for ATP is 1.2fold lower than wild-type value
N62G/K193G
Crassostrea sp.
-
turnover number is 51% of the wild-type value, KM-value for L-arginine is 4.1fold higher than wild-type value, Km-value for ATP is 3.9fold higher than wild-type value
H284A
the catalytic activity is reduced significantly compared to that in wild type enzyme. The crystal structure of H284A displays several structural changes, including the alteration of D324, a hydrogen-bonding network around H284, and the disruption of pi-stacking between the imidazole group of the H284 residue and the adenine ring of ATP
E225A
-
turnover number is 0.03% of the wild-type value
E225D
-
KM-value for ADP is 2.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.14fold higher than wild-type value, turnover number is 0.24% of the wild-type value
E225Q
-
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.4fold higher than wild-type value, turnover number is 0.3% of the wild-type value
E225Q/E314Q
-
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 2.3fold higher than wild-type value, turnover number is 0.2% of the wild-type value
E314D
-
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.56fold higher than wild-type value, turnover number is 1.7% of the wild-type value
E314Q
-
KM-value for ADP is 1.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.1fold higher than wild-type value, turnover number is 0.3% of the wild-type value
R312G/E314V/H315D/E317A/E319V
-
KM-value for ADP is 1.5fold lower than the wild-type value, KM-value for N-phospho-L-arginine is 1.5fold higher than wild-type value, turnover number is 83% of the wild-type value
R330K
the mutant enzyme is more susceptible to oxidation than the wild type enzyme and shows 20% of wild type activity
I121D
-
the mutation leads to pronounced loss of activity and structural stability. The mutation also leads to serious aggregation during heat-and guanidine hydrochloride-induced denaturation and refolding from the guanidine hydrochloride-denatured state
I121G
-
the mutation leads to pronounced loss of activity and structural stability. The mutation also leads to serious aggregation during heat-and guanidine hydrochloride-induced denaturation and refolding from the guanidine hydrochloride-denatured state
I121K
-
the mutation leads to pronounced loss of activity and structural stability. The mutation also leads to serious aggregation during heat-and guanidine hydrochloride-induced denaturation and refolding from the guanidine hydrochloride-denatured state
I121L
-
the almost has no effect on AK activity and structural stability
L113D
the mutant shows strongly decreased activity compared to the wild type enzyme
L113G
the mutant shows decreased activity compared to the wild type enzyme
L113I
the mutant shows about wild type Km and kcat values
L113K
the mutant shows strongly decreased activity (10.3% catalytic efficiency) compared to the wild type enzyme
P272D
-
activity of the mutant P272D is about 40% of that of wild-type enzyme. The binding affinity of arginine and ATP in the P272D is much smaller than that of wild-type enzyme, as indicated by an about 2- to 3fold increase of the Km values for ATP and arginine. The mutation impairs the tertiary structures of the enzyme. Decrease in thermal stability
T273A
site-directed mutagenesis, the mutation leads to significant loss of activity, obviously decreased substrate synergism and structural stability compared to the wild-type enzyme, the enzyme structure is impaired and the enzyme protein in a partially unfolded state
T273D
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity and structure
T273G
site-directed mutagenesis, the mutation leads to significant loss of activity, obviously decreased substrate synergism and structural stability compared to the wild-type enzyme, the enzyme structure is impaired and the enzyme protein in a partially unfolded state
T273S
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity and structure
Y75D
-
mutant shows strong synergism. Fluorescence spectrum shows a red shift
Y75D/P272R
-
characteristics similar to those of the wild-type enzyme
Y75F
-
mutant shows strong synergism. Fluorescence spectrum shows a red shift
Y75F/P272G
-
the synergism is almost completely lost. Fluorescence spectrum shows a red shift
D62E
-
the mutant retains almost 90% of the wild type activity
D62G
-
the mutant has a pronounced loss in activity
R193G
-
the mutant has a pronounced loss in activity
R193K
-
the mutant retains almost 90% of the wild type activity
D62E
3.3% of Vmax of recombinant wild-type enzyme, Km-value for L-Arg is 99% of that of the wild-type enzyme
D62G
0.6% of Vmax of recombinant wild-type enzyme
R193G
1.5% of Vmax of recombinant wild-type enzyme
S63G
5.1% of Vmax of recombinant wild-type enzyme, Km-value for L-Arg is 516% of that of the wild-type enzyme
S63T
0.3% of Vmax of recombinant wild-type enzyme
Y68S
mutant enzyme without activity
D77A
-
arginine kinase AK3, Km-value for L-arginine is lower than wild-type value. Ki-value for L-arginine is 1.9 fold higher than the wild-type value
D78A
-
arginine kinase AK3, Km-value for L-arginine is higher than wild-type value. Ki-value for L-arginine is 1.14fold higher than the wild-type value
G298R
-
arginine kinase AK3, enzymatic activity is significantly reduced. Ki-value for L-arginine is 1.8fold higher than the wild-type value
Q80S
-
arginine kinase AK3, Km-value for L-arginine is lower than wild-type value. Ki-value for L-arginine is 2.2fold higher than the wild-type value
R298G
-
arginine kinase AK4, enzymatic activity of the mutant arginine kinase AK4 is comparable with that of the wild-type arginine kinase AK3. Ki-value for L-arginine is 3.8fold higher than the wild-type value
C271A
Pleocyemata sp.
-
1300fold decrease in turnover number, in presence of 1 mM Cl-. 3.6fold increase in Km-value for N-phospho-L-arginine, 7.5fold increase in Km-value for ATP, in presence of 1 mM Cl-
C271D
Pleocyemata sp.
-
86.7fold decrease in turnover number, in presence of 1 mM Cl-. 9.8fold increase in Km-value for N-phospho-L-arginine, 2.5fold increase in Km-value for ATP, in presence of 1 mM Cl-
C271N
Pleocyemata sp.
-
4727fold decrease in turnover number, in presence of 1 mM Cl-. 2.7fold increase in Km-value for N-phospho-L-arginine, 4.3fold increase in Km-value for ATP, in presence of 1 mM Cl-
C271S
Pleocyemata sp.
-
1486fold decrease in turnover number in presence of 1 mM Cl-. 16.8fold increase in Km-value for N-phospho-L-arginine, 5fold increase in Km-value for ATP in presence of 1 mM Cl-
G54A
-
the mutant shows considerably increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme
G54I
-
the mutant displays undetectable enzymatic activity
G54L
-
the mutant displays undetectable enzymatic activity
G54S
-
the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme
G54V
-
the mutant displays undetectable enzymatic activity
L64A
-
the mutant displays undetectable enzymatic activity
L64G
-
the mutant displays undetectable enzymatic activity
L64I
-
in the mutant, the affinity for L-arginine is greatly increased (9.5fold that of the wild type), whereas its affinity for D-arginine is increased 2.9fold
L64V
-
the mutant shows a 1.7fold decrease in affinity for L-arginine, but unchanged affinity for D-arginine
N320A
-
the mutant shows considerably reduced enzymatic activity (17.1% for L-arginine and 5.19% for D-arginine compared to the wild type enzyme)
N320D
-
the mutant shows considerably reduced enzymatic activity (32.4% for L-arginine and 48.4% for D-arginine compared to the wild type enzyme)
N320E
-
the mutant shows considerably reduced enzymatic activity (52.3% for L-arginine and 10.1% for D-arginine compared to the wild type enzyme)
N320H
-
the mutant shows considerably reduced enzymatic activity (29.5% for L-arginine and 10.2% for D-arginine compared to the wild type enzyme)
N320K
-
the mutant shows considerably reduced enzymatic activity (0.612% for L-arginine and 0.489% for D-arginine compared to the wild type enzyme)
N320Q
-
the mutant shows considerably reduced enzymatic activity (8.97% for L-arginine and 2,6% for D-arginine compared to the wild type enzyme)
N320R
-
the mutant shows considerably reduced enzymatic activity (4.11% for L-arginine and 1.46% for D-arginine compared to the wild type enzyme)
Y89Q
-
the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme
E314V
-
turnover number is 0.000019% of the wild-type value
E314V
-
significantly decreased activity
P272G
-
decrease in thermal stability
P272G
-
the synergism is almost completely lost. Fluorescence spectrum shows a red shift
P272R
-
decrease in thermal stability
P272R
-
the synergism is almost completely lost. Fluorescence spectrum shows a red shift
Q80A
-
arginine kinase AK3, Km-value for L-arginine is lower than wild-type value. Ki-value for L-arginine is 1.5fold higher than the wild-type value
Q80A
-
the SES complex dissociation constant (Ki SES: 0.64 mM) is two times larger than that of the wild-type as well as the ES complex dissociation constant (Ki ES: 0.29 mM). The regression curve for this mutant resembles that of the wild-type, suggesting that substrate inhibition is still present in this mutant
S79A
-
arginine kinase AK3, loss of substrate inhibition by L-arginine. Ki-value for L-arginine is 8.3fold higher than the wild-type value
S79A
-
the SES complex dissociation constant (Ki SES: 3.62 mM) is ten times than that of the wild-type (0.34 mM). This suggests the significant involvement of the S79 residue in binding processes at the second arginine substrate, i.e., in displaying substrate inhibition
V81A
-
arginine kinase AK3, Km-value for L-arginine is higher than wild-type value. Ki-value for L-arginine is 12.2 fold higher than the wild-type value
V81A
-
the SES complex dissociation constant (Ki SES: 2.16 mM) is significantly larger (seven times) than that of the wildtype, similar to the S79A mutant. The regression curve also resembles that of the S79A mutant, indicating that substrate inhibition is not absent, but rather weakened
additional information
-
the kcat value of the mutant with six Lys residues in the linker region between domains D1 and D2 is reduced to 27.6% that of the two-domain wild-type enzyme
additional information
-
deletion mutants of arginine kinase are constructed. The first 4, 6, 8 and 10 amino acids of the N-terminal are deleted. The deletion mutants assume less compact conformations compared to the wild-type, whereas no significant changes of the secondary or the quaternary structures are observed, implying that the deletions cause a perturbation in the tertiary structure or the hydrodynamic properties of the enzyme. The enzymatic and denaturing measurements show that removal of the N-terminal residues decrease the activity and stability of the enzyme markedly. The instability increases in accord with the increased number of amino acid residues removed from the N-terminal of the enzyme
additional information
-
double mutant Val268insertion/Phe270deletion: enzyme with significaltly decreased specific activity compared with both the native and the recombinant wild-type enzyme, no detectable change in guanidine substrate specificity
additional information
effects of the enzyme mutations on the enzyme's thermal inactivation andaggregation, the mutant enzymes show reduced thermal stability compared to the wild-type enzyme, overview
additional information
generation of a stable isozyme AK1 knockout DELTAak1 line
additional information
-
generation of a stable isozyme AK1 knockout DELTAak1 line
additional information
generation of tetracycline-inducible PCF TbAK-RNAi cell line which allows the simultaneous silencing of all three TbAK isoforms. The TbAK-depleted cell line becomes about 400fold more sensitive to hydrogen peroxide
additional information
generation of tetracycline-inducible PCF TbAK-RNAi cell line which allows the simultaneous silencing of all three TbAK isoforms. The TbAK-depleted cell line becomes about 400fold more sensitive to hydrogen peroxide
additional information
generation of tetracycline-inducible PCF TbAK-RNAi cell line which allows the simultaneous silencing of all three TbAK isoforms. The TbAK-depleted cell line becomes about 400fold more sensitive to hydrogen peroxide
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
generation of tetracycline-inducible PCF TbAK-RNAi cell line which allows the simultaneous silencing of all three TbAK isoforms. The TbAK-depleted cell line becomes about 400fold more sensitive to hydrogen peroxide
-
additional information
-
generation of tetracycline-inducible PCF TbAK-RNAi cell line which allows the simultaneous silencing of all three TbAK isoforms. The TbAK-depleted cell line becomes about 400fold more sensitive to hydrogen peroxide
-
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AK3 is synthesized using a cell-free protein synthesis system
amplification of cDNA for arginine kinase
amplification of cDNA for arginine kinase. There are three unique arginine kinase genes in the choanoflagellate Monosiga brevicollis
cDNAs of the two-domain arginine kinase and its separated domains 1 and 2 from Anthopleura japonicus, are cloned into the plasmid pMAL, and recombinant enzymes are expressed in Escherichia coli as MBP fusion proteins
cloned in prokaryotic expression plasmid pET-28a, and then expressed in Escherichia coil strain Rosetta in dissoluble form
cloned it in pMAL plasmid and expressed it in Escherichia coli as a fusion protein with maltose-binding protein
cloning of cDNAs into pMAL plasmid and expression in Escherichia coli as a fusion protein with MBP tag or hexameric His tag
DNA and amino acid sequence determination and analysis, sequence comparisons
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
-
domain 2 is separated from the two-domain enzyme and expressed in Escherichia coli, domain 2 still exhibits activity. Expression of mutants of domain 2 in Escherichia coli: H60G, H60R and D197G
-
expressed as a fusion protein with maltose-binding protein in Escherichia coli JM109 cells
-
expressed as a fusion protein with maltose-binding protein in Escherichia coli TB1 cells
expressed as a His-tagged fusion protein in Escherichia coli BL21 cells
expressed as fusion proteins with the maltose-binding protein in Escherichia coli. When expressed alone, domain 1 displays minimal activity. When expressed alone, domain 2 has significantly higher activity and catalytic efficiency that the two-domain wild-type AK, when domain 1 is inactivated using the Y68A mutation, activity is about 50% of the wild-type enzyme and when domain 2 is inactivated using the Y68A mutation, activity is retained at about 12% of the wild-type level
expressed as maltose-binding protein enzyme fusion protein in Escherichia coli TB-1 cells
-
expressed in Escherichia coli
expressed in Escherichia coli as a fusion protein with maltose-binding protein
expressed in Escherichia coli as a fusion with maltose-binding protein
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 (DE3) codon plus cells by prokaryotic expression plasmid pGEX-4T-2 as glutathione S-transferase arginine kinase fusion protein
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Codon Plus cells
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli by two prokaryotic expression plasmids, pET-30a and pET-28a28a. The recombinant protein is expressed as inclusion bodies using pET-30a. Using expression plasmid, pET-28a, and changing the expression conditions results in a soluble and functional form of arginine kinase
expressed in Escherichia coli M15 cells
expressed in Escherichia coli Rosetta cells
expressed in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli
expression in Escherichia coli as a histidine-tagged protein
-
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21(DE3) Rosetta
expression of Cissites arginine kinase protein in Escherichia coli as a fusion with maltose-binding protein
expression of wild-type and mutant enzymes (Y75F, Y75D, P272G, P272R, Y75F/P272G and Y75D/P272R) in Escherichia coli BL21 (DE3)
-
gene AK1 or Tb927.9.6170, located on chromosome 9, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression of full-length and truncated versions of epitope tagged isozyme AK1
gene AK1, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His6-tagged isozyme AK1 in Escherichia coli strain BL21 (DE3). The prokaryotic protein expression host Escherichia coli uses the standard genetic code while Tetrahymena pyriformis uses an alternative genetic code where TAA and TAG code for glutamine instead of a stop codon, therefore a TAA codon in AK1 is replaced with CAA
gene AK2, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His6-tagged isozyme AK2 in Escherichia coli strain BL21(DE3). The prokaryotic protein expression host Escherichia coli uses the standard genetic code while Tetrahymena pyriformis uses an alternative genetic code where TAA and TAG code for glutamine instead of a stop codon., therefore two TAA and three TAG codons in AK2 are replaced with CAA and CAG
gene argk-1, DNA and amino acid sequence determination and analysis, sequence comparisons, molecular genetic and phylogenetic analysis
gene cloned and inserted into the prokaryotic expression plasmid pET-21b, expression in a soluble and functional form in Escherichia coli
-
gene HcAK, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of soluble N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Tb09.160.4560, sequence comparisons of Trypanosoma brucei isozymes AK1-3, recombinant expression of N-terminally His-tagged isozyme in Escherichia coli strain BL21(DE3)
gene Tb927.9.6230, sequence comparisons of Trypanosoma brucei isozymes AK1-3
gene TbAK3, sequence comparisons of Trypanosoma brucei isozymes AK1-3
gene TcAK, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of soluble N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene YH65_02995, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
isoform AK2 fused to maltose-binding protein is expressed in Escherichia coli TB1 cells
-
open reading frame of Toxocara canis arginine kinase is cloned into the BamHI/SalI site of pMAL-c2X. The maltose-binding protein (MBP)-Toxocara canis arginine kinase fusion protein is expressed in Escherichia coli TB1 cells by induction with 1 mM IPTG at 25°C for 24 h
-
recombinant expression of His-tagged enzyme in Escherichia coli strain Rossta
-
recombinant expression of His6-tagged isozyme AK1 in Escherichia coli strain TB1
recombinant expression of His6-tagged isozyme AK2 in Escherichia coli strain TB1
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
the His6-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
-
-
amplification of cDNA for arginine kinase
amplification of cDNA for arginine kinase
amplification of cDNA for arginine kinase
amplification of cDNA for arginine kinase
amplification of cDNA for arginine kinase
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
expressed in Escherichia coli BL21(DE3) Codon Plus cells
expressed in Escherichia coli Rosetta cells
expressed in Escherichia coli Rosetta cells
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Pleocyemata sp.
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
-
expression in Escherichia coli BL21 (DE3)
-
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