Information on EC 2.7.3.3 - arginine kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.7.3.3
-
RECOMMENDED NAME
GeneOntology No.
arginine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-arginine Nomega-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-70-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Crassostrea sp.
-
-
-
Manually annotated by BRENDA team
cat flea
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Southern pink shrimp
-
-
Manually annotated by BRENDA team
Indian white prawn
-
-
Manually annotated by BRENDA team
Banana prawn
-
-
Manually annotated by BRENDA team
gene HcAK
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Isostychopus badonotus
sea cucumber
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Australian sheep blowfly
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Northern shrimp
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
giant tiger prawn
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Pleocyemata sp.
-
-
-
Manually annotated by BRENDA team
Argentine red shrimp
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-
Manually annotated by BRENDA team
Portunus sp.
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
mud crab
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-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene YH65_02995
UniProt
Manually annotated by BRENDA team
gene TcAK
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + Nomega-phospho-L-Arg
ATP + L-Arg
show the reaction diagram
-
-
-
r
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
show the reaction diagram
-
-
-
-
?
ADP + omega-N-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
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
show the reaction diagram
-
8% of the activity with L-Arg
-
-
?
ATP + 5-guanidinopentanoic acid
ADP + N-phospho-5-guanidinopentanoic acid
show the reaction diagram
-
10% of the activity with L-Arg
-
-
?
ATP + CtsR-L-Arg
ATP + CtsR-N-phospho-L-Arg
show the reaction diagram
-
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
show the reaction diagram
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
show the reaction diagram
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
show the reaction diagram
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
show the reaction diagram
ATP + L-arginine ethyl ester
ADP + Nomega-phospho-L-Arg ethyl ester
show the reaction diagram
6% activity compared to L-Arg
-
-
?
ATP + L-arginine methyl ester
ADP + Nomega-phospho-L-arginine methyl ester
show the reaction diagram
-
-
-
-
?
ATP + L-arginine-O-ethyl ester
?
show the reaction diagram
-
isoform arginine kinase 2 shows about 16% activity of that obtained with L-Arg
-
-
?
ATP + L-argininic acid
ADP + Nomega-phospho-L-argininic acid
show the reaction diagram
-
45% of the activity with L-Arg
-
-
?
ATP + L-canavanine
?
show the reaction diagram
about 16% activity compared to L-Arg
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
show the reaction diagram
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
show the reaction diagram
ATP + lombricine
ADP + omega-N-phospholombricine
show the reaction diagram
ATP + N-acetyl-L-Arg
ADP + Nomega-phospho-N-alpha-acetyl-L-Arg
show the reaction diagram
-
13% of the activity with L-Arg
-
-
?
ATP + octopine
ADP + N-phospho-D-octopine
show the reaction diagram
-
30% of the activity with L-Arg
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
GDP + Nomega-phospho-L-Arg
GTP + L-Arg
show the reaction diagram
-
10% of the activity with ADP
-
-
?
GTP + L-arginine
GDP + Nomega-phospho-L-arginine
show the reaction diagram
UDP + Nomega-phospho-L-Arg
UTP + L-Arg
show the reaction diagram
-
10% of the activity with ADP
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
show the reaction diagram
Q4AED1, Q4AED2
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sn2+
-
4 mM, 13% of the activation with Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
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
-
-
Ag+
-
dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+
agmatine
aminoguanidine
-
10 mM, 2.6% inhibition
aspartate
-
0.02-0.15 mM, causes inactivation and unfolding of arginine kinase
canavanine
chloride
citrulline
Creatine
D-Arg
D-arginine
-
competitive
D-glucose
the enzyme is inhibited by 50 mM D-glucose, almost all arginine kinase activity is lost after treatment with 200 mM D-glucose
dithiothreitol
-
conformational change and inactivation
DTNB
-
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course. This reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site
Ethylguanidine
-
5fold higher concentration than L-Arg, 22% inhibition
glutamate
glycine
guanidine
guanidine butyrate
-
10 mM, 4.3% inhibition
guanidine hydrochloride
His
-
5fold higher concentration than L-Arg, 50% inhibition
homoarginine
-
10 mM, 38.2% inhibition
Iodide
iodoacetamide
-
-
isoleucine
K+
-
200 mM, 50% inhibition
L-arginine
-
-
L-arginine methyl ester
-
competitive to L-Arg
L-Asp
-
5fold higher concentration than L-Arg, 25% inhibition
L-canavanine
L-Glu
-
5fold higher concentration than L-Arg, 31% inhibition
L-Glucose
AK-1 activity does not show significant variation after supplementation with 10 mM L-glucose. However, AK-1 activity decreases significantly when L-glucose concentration is higher than 50 mM and almost all MrAK-1 activity is lost after treatment with 200 mM L-glucose
L-histidine
-
10 mM, 2.4% inhibition
L-homoarginine
-
5fold higher concentration than L-Arg, 33% inhibition
L-Lys
-
5fold higher concentration than L-Arg, 25% inhibition
L-nitroarginine
lysine
Mg2+
-
at high concentrations noncompetitive inhibition of MgATP2-
MgADP-
-
inhibition is potentiated by NO3-
MgATP2-
-
enzyme form AK2 is strongly inhibited at high concentrations
Mn2+
-
at high concentrations noncompetitive inhibition of MgATP2-
N-methyl-L-Arg
-
5fold higher concentration than L-Arg, 28% inhibition
Na+
-
200 mM, 50% inhibition
NADH
-
noncompetitive
NH4+
-
200 mM, 50% inhibition
nitrate
nitrite
nitroarginine
ornithine
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal
putrescine
rutin
SDS
complete inactivation at 1.0 mM, the inactivation is a first-order reaction, with the kinetic processes shifting from a monophase to biphase as SDS concentrations increase. SDS concentrations lower than 5 mM do not induce conspicuous changes in tertiary structures, while higher concentrations of SDS exposedhydrophobic surfaces and induce conformational changes
Thiocyanate
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
Isostychopus badonotus
-
5.5% activation at 50 mM
dithiothreitol
-
once treated with 5,5'-dithiobis-2-nitrobenzoic acid, the enzyme activity can be recovered more than 95% after incubation for 20 min with 0.15 mM dithiothreitol
DMSO
-
protects arginine kinase from inactivation losing its native tertiary conformation and aggregation in the presence of guanidine hydrochloride
glycerol
-
protects arginine kinase from inactivation in both low and high concentrations of guanidine hydrochloride
hydrogen peroxide
-
produces up to 10fold increase in enzyme expression at 0.2 mM
nifurtimox
-
produces 2.3fold increase in enzyme expression at 0.01 mM
proline
-
with proline the residual activity of AK after incubation in guanidine hydrochloride is higher than without proline
Sucrose
-
maintains the activity of the enzyme in the presence of guanidine hydrochloride
additional information
-
not affected by sodium nitroprusside, methylene blue and benznidazole
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
5-guanidinopentanoic acid
-
pH 8.5, 25°C
0.0134 - 1.25
ADP
0.023 - 13.3
ATP
1.3 - 13.9
D-Arg
0.106 - 35.4
L-Arg
18
L-arginic acid
-
pH 8.5, 25°C
-
0.054 - 8.458
L-arginine
2.796
L-arginine ethyl ester
recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
6.7 - 22
L-canavanine
27
L-phosphocanavanine
-
37°C
0.09 - 0.45
MgADP-
0.14 - 1.4
MgATP2-
30
N-acetyl-L-Arg
-
-
0.63 - 1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
0.7 - 3.5
Nomega-phospho-L-Arg
15
octopine
-
pH 8.5, 25°C
0.192
omega-N-phospho-L-arginine
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 140
ADP
0.00229 - 180
ATP
2 - 121
D-Arg
0.08 - 678
L-Arg
0.00229 - 459
L-arginine
27.3
L-canvanine
Manduca sexta
-
-
-
50.7
L-phosphocanavanine
Manduca sexta
-
-
0.27 - 140
N5-(N-phosphonocarbamimidoyl)-L-ornithine
0.093 - 431
Nomega-phospho-L-Arg
1.11
omega-N-phospho-L-arginine
Desulfotalea psychrophila
-
pH 8, 25°C
additional information
additional information
Pleocyemata sp.
-
-
-