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Information on EC 2.7.3.3 - arginine kinase
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2.7.3.3 arginine kinaseSpecify your search results
Word Map
- 2.7.3.3
- creatine
- kinases
-
phosphagen
-
invertebrate
- allergen
- shrimp
- phosphoarginine
- crab
-
crustacean
- lobster
-
guanidino
- analysis
- tropomyosin
- limulus
- stichopus
- penaeus
-
shellfish
- polyphemus
- hymenoptera
-
annelid
- mgadp
- homarus
- phaseolotoxin
-
ige-binding
- phaseolicola
-
monophyly
-
phosphotransferases
-
cdna-derived
-
scylla
- paramamosain
- medicine
- diagnostics
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
adenosine 5'-triphosphate-arginine phosphotransferase, adenosine 5'-triphosphate: L-arginine phosphotransferase, AK, AK-1, AK1, AK2, AK: L-arginine phosphotransferase, arginine kinase 1, arginine kinase 2, arginine kinase-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphate-arginine phosphotransferase
-
-
-
-
adenosine 5'-triphosphate: L-arginine phosphotransferase
-
-
-
-
AK
-
-
-
-
AK1
AK2
arginine phosphokinase
-
-
-
-
ArgK
ark
ATP: arginine N-phosphotransferase
ATP: L-arginine phosphotransferase
ATP:arginine phosphotransferase
ATP:L-arginine N-phosphotransferase
ATP:L-arginine phosphotransferase
ESAK
kinase, arginine (phosphorylating)
-
-
-
-
MXAN2252 protein
Tb09.160.4560
TbAK2
TbAK3
ArgK
-
-
-
-
ATP:L-arginine N-phosphotransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
rapid equilibrium random mechanism
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
random-order, rapid equilibrium kinetic mechanism; random-order, rapid equilibrium kinetic mechanism
U3T1K4, U3T2Y2
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
the two-substrate AK kinetics is explained by a random-order, rapid-equilibrium, kinetic mechanism
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
random-order, rapid-equilibrium kinetic mechanism
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
random-order, rapid-equilibrium kinetic mechanism; random-order, rapid-equilibrium kinetic mechanism
C0STY2, C0STY3
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-arginine Nomega-phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-70-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
ATP + 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 + 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 + 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
-
-
?
GDP + Nomega-phospho-L-Arg
GTP + L-Arg
-
10% of the activity with ADP
-
-
?
UDP + Nomega-phospho-L-Arg
UTP + L-Arg
-
10% of the activity with ADP
-
-
?
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
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
D-Arg is phosphorylated to a lesser degree
-
-
-
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
7.6% of the activity with L-Arg
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
McsB acts exclusively on L-Arg residues
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
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
-
production of high-energy reserves N-phospho-L-Arg in insect muscles
-
-
?
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
100% activity
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
isoforms AK1 and AK2 are primarily active towards L-arginine
-
-
?
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
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
-
-
-
-
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
-
-
-
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
Crassostrea sp.
-
key enzyme in invertebrate energy metabolism
-
-
?
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-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
-
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
?
-
no activity with D-arginine, N-acetyl-L-arginine, agmatine, and creatine
-
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
O61367
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
-
-
-
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
-
the enzyme is involved in the storage of the high-energy phosphate reserve phosphoarginine
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
specific reversible transfer of phosphate
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
O01854, O45011, O45518, Q10454, Q27535
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
C0STY2, C0STY3
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
A0A0F6WMX1
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
U3T1K4, U3T2Y2
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
Q38EU9, Q38EV1, Q38EV2
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
Q38EV2
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
Q38EU9, Q38EV1
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
additional information
Mg2+
-
activates at concentrations greater than 1 mM, maximal effect at 1.5 mM
Mg2+
-
highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate; highest activity if the ratio Mg2+:ADP is 4:1, synthesis of ATP
Mg2+
required; required; required; required; required
Mg2+
2 mM, absolutely required, only 2% of maximal activity without Mg2+
Mg2+
-
4 mM, activation; highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate; highest activity if the ratio Mg2+:ADP is 4:1, synthesis of ATP
Mg2+
-
4 mM, activation; highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate; highest activity if the ratio Mg2+:ADP is 4:1, synthesis of ATP
Mg2+
-
divalent cation requirement is satisfied by Mg2+ or Mn2+. Km-value for Mg2+: 0.6 mM; highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate; Km: 0.6 mM
Mn2+
-
less effective than Mg2+ in activation; more effective than Mg2+ in activation
Mn2+
-
divalent cation requirement is satisfied by Mg2+ or Mn2+. Km-value for Mn2+: 0.08 mM; Km: 0.08 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Ag+
-
dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+
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
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
L-Glucose
E2JE77
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
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
2-oxoglutarate
E2JE77
the enzyme activity is inhibited at 10-200 mM
2-oxoglutarate
the enzyme activity is inhibited by 10 mM 2-oxoglutarate
D-Arg
-
product inhibition, competitive with arginine phosphate and noncompetitive withg ADP
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
additional information
arginine kinase activity does not show significant variation after incubated with 10-200 mM L-citrulline, L-ornaline, and glycerol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
ATP
-
about 80% of the activity formerly inhibited by phenylglyoxal is retained by incubating with 20 mM ATP
ATP
after treatment with 10 mM ATP, the enzyme activity significantly increases
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.796
L-arginine ethyl ester
recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
0.16
ADP
-
mutant enzyme E225Q; mutant enzyme E225Q/E314Q; mutant enzyme E314S
0.023
ATP
pH 8.0, 25°C, recombinant enzyme
0.16
ATP
pH 8.0, 25°C, recombinant enzyme
0.23
ATP
pH 7.5, 28°C, recombinant isozyme AK1
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
0.32
ATP
pH 7.5, 37°C, recombinant isozyme AK1
0.35
ATP
pH 8.0, 25°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
0.654
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
U3T1K4, U3T2Y2
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1; 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
0.774
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
0.926
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; pH 8, 25°C
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
1.26
ATP
pH 8.0, 25°C, recombinant enzyme
1.27
ATP
-
recombinant 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
1.36
ATP
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C
1.42
ATP
-
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C
1.59
ATP
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
2.99
ATP
-
wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°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
3.72
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
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
9.34
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
0.12
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
0.18
L-Arg
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°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
0.421
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.94
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75F; 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
0.951
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 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; pH 8, 25°C
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
2.72
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
2.98
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
3.69
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
0.054
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.24
L-arginine
pH 7.5, 28°C, recombinant isozyme AK1
0.35
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G; pH 7.9, 25°C, wild-type enzyme
0.37
L-arginine
pH 8.0, 25°C, recombinant 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
0.48
L-arginine
pH 7.5, 37°C, recombinant isozyme AK1
0.88
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.92
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q/E314Q
1.166
Nomega-phospho-L-Arg
native enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
1.432
Nomega-phospho-L-Arg
recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
additional information
additional information
-
Michaelis-Menten kinetic analysis, overview. The enzyme shows a random-order, rapid equilibrium kinetic mechanism; 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; Michaelis-Menten kinetic analysis, overview. The enzyme shows a random-order, rapid equilibrium kinetic mechanism
-
additional information
additional information
U3T2Y2
Michaelis-Menten kinetic analysis, overview. The enzyme shows a random-order, rapid equilibrium kinetic mechanism; 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; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview; steady-state kinetic analysis, sequential ternary kinetic model, overview
-
additional information
additional information
-
bisubstrate kinetics and binary dissociation constants, overview
-
additional information
additional information
kinetics, overview
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
-
dissociation consants of wild-type and mutant enzymes, overview
-
additional information
additional information
determination of activation energy for transition state of AK reactions, thermodynamics; determination of activation energy for transition state of AK reactions, thermodynamics
-
additional information
additional information
C0STY3
determination of activation energy for transition state of AK reactions, thermodynamics; determination of activation energy for transition state of AK reactions, thermodynamics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.4
ATP
pH 8.0, 25°C, recombinant enzyme
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
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
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
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
45
ATP
pH 8.0, 25°C, recombinant enzyme
50.1
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
60.7
ATP
-
isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
61.8
ATP
-
isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
129
ATP
recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains
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; 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
2.02
L-Arg
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C; pH 8, 25°C
29.93
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°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
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
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
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
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
11.4
L-arginine
pH 8.0, 25°C, recombinant enzyme
40
L-arginine
pH 8.0, 25°C, recombinant enzyme
45
L-arginine
pH 8.0, 25°C, recombinant enzyme
88
L-arginine
pH 8.0, 25°C, recombinant wild-type enzyme
180
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.27
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q/E314Q
116
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.52
D-Arg
-
wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25°C
9.29
D-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C
9.52
D-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C
9.54
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
27.5
D-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
29
D-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
9.65
L-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C
12.5
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
15.4
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
39.5
L-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C
44.7
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
195
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
241
L-Arg
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
352
L-Arg
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
31
L-arginine
pH 8.0, 25°C, recombinant enzyme
45
L-arginine
pH 8.0, 25°C, recombinant enzyme
440
L-arginine
pH 8.0, 25°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE