Information on EC 2.7.3.3 - arginine kinase

New: Word Map on EC 2.7.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
-
-
-
-
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
-
-
-
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
-
-
-
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
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
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Isostychopus badonotus
sea cucumber
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
-
-
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
-
UniProt
Manually annotated by BRENDA team
-
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
giant tiger prawn
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Pleocyemata sp.
-
-
-
Manually annotated by BRENDA team
Argentine red shrimp
-
-
Manually annotated by BRENDA team
Portunus sp.
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
mud crab
-
-
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
-
-
-
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
physiological function
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
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
activates
Sn2+
-
4 mM, 13% of the activation with Mg2+
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
Creatine
-
10 mM, 12.7% inhibition
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
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
-
-
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
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
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal
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
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, 25C
0.0134 - 1.25
ADP
0.3 - 13.3
ATP
1.3 - 13.9
D-Arg
0.106 - 35.4
L-Arg
18
L-arginic acid
-
pH 8.5, 25C
-
0.307 - 8.458
L-arginine
2.796
L-arginine ethyl ester
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22C
6.7 - 22
L-canavanine
27
L-phosphocanavanine
-
37C
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, 25C
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 - 163
ATP
2 - 121
D-Arg
0.08 - 678
L-Arg
0.00229 - 212.9
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, 25C
additional information
additional information
Pleocyemata sp.
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.52 - 29
D-Arg
9.65 - 352
L-Arg
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028
Ag+
-
at 25C in 50 mM Tris-HCl buffer (pH 7.0)
7.55
canavanine
-
-
0.31
D-arginine
-
-
6.02
homoarginine
-
-
6
L-canavanine
-
pH 7.3, 30C
7
L-homoarginine
-
pH 7.3, 30C
8
nitrate
-
with L-arginine as substrate
0.008
rutin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
Ag+
Fenneropenaeus chinensis
-
at 25C in 50 mM Tris-HCl buffer (pH 7.0)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00227
-
formation of arginine phosphate, enzyme from crude extract
0.00312
-
formation of ATP, enzyme from crude extract
0.245
-
homogenous muscle enzyme
0.2539
-
cell extract
0.288
-
cell extract
8.78
at pH 8.6 and 30C
53.78
-
mutant enzyme R330K, pH and temperature not specified in the publication
268.6
-
recombinant wild type enzyme, pH and temperature not specified in the publication
390.5
-
after purification
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
synthesis of ATP
6.1
-
synthesis of ATP
6.2 - 6.3
-
synthesis of ATP
6.3
-
synthesis of ATP, 20 mM phosphate buffer
6.5 - 7.5
-
reverse reaction
6.9
-
synthesis of ATP, 20 mM Tris-HCl buffer
7.1 - 7.2
-
synthesis of ATP
7.2
-
formation of ATP, enzyme from third stage juveniles
7.3
-
formation of ATP, enzyme from adult
7.5 - 8
-
-
7.8
-
formation of arginine phosphate, enzyme from third-stage juveniles
7.9 - 8.5
-
formation of arginine phosphate, enzyme from adult
8.3
-
synthesis of N-phospho-L-arginine
8.7 - 8.8
-
synthesis of N-phospho-L-arginine
9
-
synthesis of N-phospho-L-arginine
9.2
-
synthesis of N-phospho-L-arginine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.2
-
pH 5.0: about 30% of maximal activity, pH 8.2: about 30% of maximal activity, ATP synthesis
5.5 - 8
5.5 - 7.5
-
pH 5.5: about 90% of maximal activity, pH 7.5: about 60% of maximal activity, synthesis of ATP
5.6 - 7.5
-
about 15% of maximal activity, pH 5.6: about 85% of maximal activity, pH 7.5: about 80% of maximal activity, synthesis of arginine and ATP; pH 5.3
5.9 - 6.8
-
pH 5.9: about 35% of maximal activity, pH 6.8: about 55% of maximal activity, synthesis of ATP, 20 mM phosphate buffer
6.3 - 9
-
pH 6.3: about 65% of maximal activity, pH 9.0: about 70% of maximal activity, synthesis of N-phospho-L-Arg
6.5 - 7.3
-
pH 6.5: about 45% of maximal activity, pH 9.0: about 45% of maximal activity, synthesis of ATP, 20 mM Tris-HCl buffer
7 - 10.5
-
pH 7.0: about 40% of maximal activity, pH 10.5: about 35% of maximal activity, synthesis direction of phosphoarginine and ADP
7 - 10
-
pH 7.0, about 30% of maximal activity, pH 10.0: about 35% of maximal activity, synthesis of N-phospho-L-arginine
7.2 - 9
-
pH 7.2: about 45% of maximal activity, pH 9.0: about 55% of maximal activity, synthesis of arginine phosphate and ADP
7.5 - 9
-
about 50% of maximal activity at pH 7.5 and pH 9.0, synthesis of N-phospho-L-arginine, 20 mM Tris-HCl buffer
8 - 10.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
synthesis of ATP and synthesis of N-phospho-L-Arg
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 70
-
10C: about 55% of maximal activity, 70C: about 40% of maximal activity, synthesis direction of phosphoarginine and ADP
10 - 60
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
calculated from sequence
5.82
-
theoretical value calculated from amino acid sequence
6.1
calculated from amino acid sequence
6.21
calculated from sequence of cDNA
6.7
calculated from sequence
7
-
theoretical value calculated from amino acid sequence
7.1
calculated from amino acid sequence
7.2
calculated from sequence
8.28
calculated from sequence
8.38
calculated from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
male and female
Manually annotated by BRENDA team
subcuticular skin, lowest mRNA expression in the skin
Manually annotated by BRENDA team
the enzyme is more abundant in the thorax, where it represents up to 2% of the total soluble protein, compared to head or abdomen
Manually annotated by BRENDA team
additional information