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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
-
phosphagen
- allergen
- shrimp
- phosphoarginine
-
crustacean
- crab
- tropomyosin
- lobster
-
guanidino
- analysis
- limulus
-
shellfish
- penaeus
- hymenoptera
-
ige-binding
- stichopus
- phaseolicola
- mgadp
-
monophyly
- taurocyamine
-
phosphotransferases
- polyphemus
-
cdna-derived
- phaseolotoxin
- homarus
- scylla
-
pan-allergens
- paramamosain
- medicine
- diagnostics
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
arginine kinase, argk, arginine phosphokinase, pyak3, tcak1, mnak2, tcak2, tbak3, pyak2, pyak4, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphate-arginine phosphotransferase
-
-
-
-
adenosine 5'-triphosphate: L-arginine phosphotransferase
-
-
-
-
AK
-
-
-
-
AK1
AK2
AK3
arginine kinase 2
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
Apis mellifera
-
-
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
Tetrahymena pyriformis
-
-
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
Sulfurovum lithotrophicum
-
-
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
Neocaridina denticulata
-
-
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
Myzostoma cirriferum
-
-
-
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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
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 + 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
ADP + ?
arginine kinase TcAK1 shows approximately 15% reaction rate compared to L-arginine
-
-
?
ATP + L-Nalpha-acetylarginine
ADP + ?
arginine kinase TcAK1 shows approximately 15% reaction rate compared to L-arginine
-
-
?
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
-
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
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
-
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
-
enzymatic activity of arginine kinase AK4 is less by 3% than that of arginine kinase AK3
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-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
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
-
-
-
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
?
-
-
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
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
-
-
-
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
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
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
Mg2+
2 mM, absolutely required, only 2% of maximal activity without Mg2+
Mg2+
-
highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate
Mg2+
-
highest activity if the ratio Mg2+:ADP is 4:1, synthesis of ATP
Mg2+
-
highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate
Mg2+
-
divalent cation requirement is satisfied by Mg2+ or Mn2+. Km-value for Mg2+: 0.6 mM
Mg2+
-
highest activity if ratio Mg2+:ATP is 1:1, synthesis of arginine phosphate
Mn2+
-
divalent cation requirement is satisfied by Mg2+ or Mn2+. Km-value for Mn2+: 0.08 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic 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
Ag+
-
dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+
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
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
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-homoarginine
5fold higher concentration than L-Arg, 33% inhibition
N-methyl-L-Arg
5fold higher concentration than L-Arg, 28% inhibition
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
D-Arg
-
product inhibition, competitive with arginine phosphate and noncompetitive withg ADP
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-nitroarginine
5fold higher concentration than L-Arg, 28% inhibition
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
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
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Asthma
Expression in Escherichia coli and Purification of Folded rDer p 20, the Arginine Kinase From Dermatophagoides pteronyssinus: A Possible Biomarker for Allergic Asthma.
Asthma
Mite-Induced Asthma and IgE Levels to Shrimp, Mite, Tropomyosin, Arginine Kinase, and Der p 10 Are the Most Relevant Risk Factors for Challenge-Proven Shrimp Allergy.
Chagas Disease
Arginine kinase of the flagellate protozoa Trypanosoma cruzi. Regulation of its expression and catalytic activity.
Chagas Disease
IgE antibodies against Trypanosoma cruzi arginine kinase in patients with chronic Chagas disease.
Chagas Disease
Resveratrol inhibits Trypanosoma cruzi arginine kinase and exerts a trypanocidal activity.
Chagas Disease
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites.
Coinfection
The Flagellar Arginine Kinase in Trypanosoma brucei Is Important for Infection in Tsetse Flies.
Food Hypersensitivity
Proteome mining for novel IgE-binding proteins from the German cockroach (Blattella germanica) and allergen profiling of patients.
Food Hypersensitivity
T cell epitope of arginine kinase with CpG co-encapsulated nanoparticles attenuates a shrimp allergen-induced Th2-bias food allergy.
Hypersensitivity
Identification of Allergenic Epitopes and Critical Amino Acids of Major Allergens in Chinese Shrimp ( Penaeus chinensis) by Immunoinformatics Coupled with Competitive-Binding Strategy.
Hypersensitivity
Induction of mud crab (Scylla paramamosain) tropomyosin and arginine kinase specific hypersensitivity in BALB/c mice.
Hypersensitivity
Mite-Induced Asthma and IgE Levels to Shrimp, Mite, Tropomyosin, Arginine Kinase, and Der p 10 Are the Most Relevant Risk Factors for Challenge-Proven Shrimp Allergy.
Hypersensitivity
Periplaneta americana arginine kinase as a major cockroach allergen among Thai patients with major cockroach allergies.
Hypersensitivity
Purification, cloning, expression and immunological analysis of Scylla serrata arginine kinase, the crab allergen.
Hypersensitivity
Shrimp allergy beyond Tropomyosin in Italy: clinical relevance of Arginine Kinase, Sarcoplasmic calcium binding protein and Hemocyanin.
Hypersensitivity
The effect of immunotherapy on cross-reactivity between house dust mite and other allergens in house dust mite -sensitized patients with allergic rhinitis.
Infections
A hypothetical model of crossing Bombyx mori nucleopolyhedrovirus through its host midgut physical barrier.
Infections
Arginine kinase is highly expressed in a resistant strain of silkworm (Bombyx mori, Lepidoptera): Implication of its role in resistance to Bombyx mori nucleopolyhedrovirus.
Infections
Discovery of the genes in response to white spot syndrome virus (WSSV) infection in Fenneropenaeus chinensis through cDNA microarray.
Infections
Proteomic analysis of differentially expressed proteins in Penaeus monodon hemocytes after Vibrio harveyi infection.
Infections
Sero-detection of Toxocara canis infection in human with T.canis recombinant arginine kinase, cathepsin L-1 and TES-26 antigens.
Infections
The Flagellar Arginine Kinase in Trypanosoma brucei Is Important for Infection in Tsetse Flies.
Larva Migrans, Visceral
Development of a highly sensitive IgG-ELISA based on recombinant arginine kinase of Toxocara canis for serodiagnosis of visceral larva migrans in the murine model.
Rhinitis, Allergic
The effect of immunotherapy on cross-reactivity between house dust mite and other allergens in house dust mite -sensitized patients with allergic rhinitis.
Starvation
Arginine kinase of the flagellate protozoa Trypanosoma cruzi. Regulation of its expression and catalytic activity.
Starvation
Functional expression of phosphagen kinase systems confers resistance to transient stresses in Saccharomyces cerevisiae by buffering the ATP pool.
Trypanosomiasis
Interaction between Gallotannin and a Recombinant Form of Arginine Kinase of Trypanosoma brucei: Thermodynamic and Spectrofluorimetric Evaluation.
Trypanosomiasis
Interaction of nanoparticles with arginine kinase from Trypanosoma brucei: Kinetic and mechanistic evaluation.
Trypanosomiasis, African
Arginine kinase: a common feature for management of energy reserves in African and American flagellated trypanosomatids.
Virus Diseases
Arginine kinase of Litopenaeus vannamei involved in white spot syndrome virus infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.796
L-arginine ethyl ester
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
0.16
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
0.4
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.023
ATP
pH 8.0, 25°C, recombinant enzyme
0.23
ATP
pH 7.5, 28°C, recombinant isozyme AK1
0.32
ATP
pH 7.5, 37°C, recombinant isozyme AK1
0.35
ATP
pH 8.0, 25°C, recombinant enzyme
0.47
ATP
wild-type enzyme, pH and temperature not specified in the publication
1.59
ATP
-
isoform AK2 mutant Y89Q, using D-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
1.13
ATP
-
wild type enzyme isoform AK2, 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
1.12
ATP
-
isoform AK2 mutant G54A, using D-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
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
1.36
ATP
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C
2.38
ATP
-
mutant enzyme I121G, 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
2.42
ATP
mutant enzyme L113G, 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
1.42
ATP
mutant enzyme L113I, 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
3.72
ATP
-
isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
1.26
ATP
pH 8.0, 25°C, recombinant enzyme
1.29
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
3.56
ATP
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30°C
0.774
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.661
ATP
-
isoform AK2 mutant G54A, 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
0.926
ATP
-
isoform AK2 mutant G54S, using L-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
0.837
ATP
-
isoform AK2 mutant L64I, using D-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
3.68
ATP
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C
0.744
ATP
mutant enzyme A105S/S106G, in 4.76 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
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
6.45
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.14
D-Arg
-
isoform AK2 mutant L64I, 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
9.34
D-Arg
-
isoform AK2 mutant G54S, in 100 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
0.12
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
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
1.01
L-Arg
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C
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
0.98
L-Arg
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C
0.126
L-Arg
recombinant wild type enzyme, in 4.76 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
2.72
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.25
L-Arg
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C
2.5 - 3
L-Arg
-
mutant enzyme I121K, 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
2.05
L-Arg
-
isoform AK2 mutant G54S, 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
1.81
L-Arg
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C
1.74
L-Arg
-
mutant enzyme I121G, 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
0.389
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C
5.07
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.69
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
0.421
L-Arg
-
recombinant wild type enzyme, 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
2.726
L-Arg
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C
0.26
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
0.41
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
0.37
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
0.014
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme Q80S
0.35
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
0.076
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, wild-type enzyme
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
0.24
L-arginine
pH 7.5, 28°C, recombinant isozyme AK1
0.48
L-arginine
pH 7.5, 37°C, recombinant isozyme AK1
0.95
L-arginine
pH 8.0, 30°C, recombinant wild-type enzyme
0.88
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.124
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme G298R
0.284
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK4, mutant enzyme R298G
0.348
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme S79A
0.386
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK4, wild-type enzyme
0.558
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme V81A
0.546
L-arginine
-
25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme D78A
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
1.432
Nomega-phospho-L-Arg
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
1.166
Nomega-phospho-L-Arg
native enzyme, in 50 mM TrisHCl pH 7.5, at 22°C
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
ATP
mutant enzyme H284A, pH and temperature not specified in the publication
104
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
11.4
ATP
pH 8.0, 25°C, recombinant enzyme
45
ATP
pH 8.0, 25°C, recombinant enzyme
60.7
ATP
-
isoform AK2 mutant G54S, using D-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
180
ATP
pH 8.0, 25°C, recombinant enzyme
68.3
ATP
-
isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
18.6
ATP
wild-type enzyme, pH and temperature not specified in the publication
129
ATP
recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains
43.3
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
50.1
ATP
-
isoform AK2 mutant L64I, 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
39.5
ATP
-
wild type isoform AK2, using L-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
36.6
ATP
-
wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
33.4
ATP
-
isoform AK2 mutant Y89Q, using L-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
63.4
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
61.8
ATP
-
isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
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
121
D-Arg
-
isoform AK2 mutant G54A, 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
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
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
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
104
L-Arg
-
wild type one-domain-enzyme D1, 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
121
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C
157
L-Arg
-
wild type one-domain-enzyme D2, in 100 mM Tris/HCl, pH 8.0 at 25°C
62.3
L-Arg
-
isoform AK2 mutant L64V, in 100 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
187
L-Arg
-
mutant two-domain-enzyme D1-Lys6-D2, in 100 mM Tris/HCl, pH 8.0 at 25°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
77.8
L-Arg
-
isoform AK2 mutant Y89Q, 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
43.3
L-Arg
mutant enzyme A105S/S106G, 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
2.02
L-Arg
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C
45.9
L-Arg
recombinant wild type enzyme, in 4.76 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
152.2
L-Arg
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C
151.2
L-Arg
-
mutant enzyme I121L, 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
159.4
L-Arg
recombinant wild type enzyme, 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
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