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Enzyme Nomenclature
Information on EC 2.7.3.3 - arginine kinase
for references in articles please use BRENDA:EC2.7.3.3
Word Map on EC 2.7.3.3
- 2.7.3.3
- creatine
-
phosphagen
-
invertebrate
- shrimp
-
allergen
- phosphoarginine
- crab
-
guanidino
- analysis
- lobster
-
crustacean
- tropomyosin
- limulus
- stichopus
- penaeus
- phaseolotoxin
-
ige-binding
-
annelid
-
phosphotransferases
-
cdna-derived
-
monophyly
- polyphemus
- hymenoptera
- homarus
- phaseolicola
- mgadp
-
scylla
- medicine
- diagnostics
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.7.3.3
-
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RECOMMENDED NAME
GeneOntology No.
arginine kinase
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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
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
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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
-
arginine kinase mainly participates in energy metabolism in invertebrates. Arginine kinase is functionally analogous to creatine kinase, EC 2.7.3.2, in vertebrates
physiological function
additional information
evolution
two putative AK genes in the genome of Tetrahymena thermophila: one is a typical AK with a 40-kDa subunit (AK1) and the other is an unusual two-domain AK2 having an 80-kDa contiguous dimer, which appears to be the result of gene duplication and subsequent fusion; two putative AK genes in the genome of Tetrahymena thermophila: one is a typical AK with a 40-kDa subunit (AK1) and the other is an unusual two-domain AK2 having an 80-kDa contiguous dimer, which appears to be the result of gene duplication and subsequent fusion
evolution
the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.; the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.; the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.; the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.; the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.
evolution
-
phylogenetic analysis of amino acid sequences of phosphagen kinases indicate that the Myzostoma AK gene lineage differs from that of the polychaete Sabellastarte spectabilis AK, which is a dimer of creatine kinase (CK) origin. It is likely that the Myzostoma AK gene lineage was lost at an early stage of annelid evolution and that Sabellastarte AK evolved secondarily from the CK gene. Analysis of evolution of phosphagen kinases of annelids with marked diversity, overview
evolution
phosphoarginine and arginine kinase are the most commonly found phosphagen and phosphagen kinase in invertebrates, such as arthropods, marine invertebrates, Haemonchus contortus larvae, the entomopathogenic nematode Steinernema carpocapsae, and the protozoan parasite Trypanosoma cruzi
evolution
phosphoarginine and arginine kinase are the most commonly found phosphagen and phosphagen kinase in invertebrates, such as arthropods, marine invertebrates, Haemonchus contortus larvae, the entomopathogenic nematode Steinernema carpocapsae, and the protozoan parasite Trypanosoma cruzi
evolution
the enzyme is widely distributed in invertebrate animals. The enzyme is also found in unicellular organisms, protists and bacteria, but its occurrence is intermittent among species. Detailed phylogenetic analysis, overview
evolution
-
the enzyme is widely distributed in various invertebrates and many lower chordates but absent in vertebrates
evolution
arginine kinase genes in trypanosomatids, phylogenetic analysis, overview
malfunction
-
larval settlement rate decreases and larval movement is inhibited in response to treatments with high concentrations of enzyme inhibitors rutin and quercetin
malfunction
RNAi knockdown of all three arginine kinase isozymes induces a growth defect that is more prominent when the cells are exposed to oxidative stress. Loss of flagellar isozyme AK1 reduces swim velocity without visible alteration of flagellar morphology. The absence of isozyme AK1 results in reduced infectivity by procyclic trypanosomes for tsetse flies
malfunction
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide; elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide; elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
malfunction
-
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide; elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
-
malfunction
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
-
physiological function
arginine kinase may play an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
arginine kinase is involved in the antiviral process of Bombyx mori larvae against nucleopolyhedrovirus infection
physiological function
the enzyme plays an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
physiological function
isozyme AK1 plays a role in the phosphoarginine shuttle, which enables a continuous energy flow to dynein for ciliary movement in Tetrahymena pyriformis
physiological function
arginine kinase plays a key role in ATP buffering systems of tissues and nerves that display high and variable rates of ATP turnover
physiological function
-
arginine kinase is a key enzyme for cellular energy metabolism, catalyzing the reversible phosphoyl transfer from phosphoarginine to ADP in invertebrates
physiological function
O004B5
arginine kinase is a key enzyme for energetic balance in invertebrates and plays an important role in invertebrate physiology by buffering the ATP pool accordingly to cellular energy requirements
physiological function
-
the enzyme is involved in the larval settlement through mediating energy supply in muscle tissues. The enzyme mainly provides energy for muscle movements and is essential for motility in arthropods
physiological function
isozyme AK1 confers a competitive advantage in infections of tsetse flies in midgut by the parasite, overview
physiological function
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide; the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide; the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
physiological function
-
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
-
physiological function
-
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide; the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
-
additional information
-
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate; the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate; the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate; the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
-
enzyme structure homology modelling, overview; residue C271 is involved in the enzyme activity and constraining the orientation of the substrate arginine. Residue T273 interacts with C271 and plays a vital role in the enzyme activity, substrate synergism, and structural stability
additional information
-
the active region of enzyme AK is more flexible than the overall enzyme molecule
additional information
the active region of enzyme AK is more flexible than the overall enzyme molecule
additional information
O004B5
the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, does not interact with arginine in the binary complex. Residue Glu324 is located in the flexible loop 310-320 that covers the active site and only stabilizes in the ternary transition state analogue complex, LvAK-TSAC
additional information
isozyme AK1 has two insertions of respectively 22 and 26 amino acids at the N- and C-terminus
additional information
O004B5
enzyme structure homology modeling and docking simulations, overview
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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
Q4AED1, Q4AED2
35.2% relative activity compared to 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 + 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
-
isoforms AK1 and AK2 are primarily active towards L-arginine
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
Q004B5
arginine kinase is an allergenic protein
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
-
synergism in substrate binding
-
-
?
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
-
-
-
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
Q4AED1, Q4AED2
0.17% of the activity with L-Arg
-
-
?
ATP + lombricine
ADP + omega-N-phospholombricine
Q4AED1, Q4AED2
3.0% 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
?
-
D5FLG2
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 SUBSTRATES
NATURAL PRODUCTS
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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INHIBITORS
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
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
the enzyme activity is inhibited by 10 mM 2-oxoglutarate
2-oxoglutarate
the enzyme activity is inhibited at 10-200 mM
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
after treatment with 10 mM ATP, the enzyme activity significantly increases
ATP
-
about 80% of the activity formerly inhibited by phenylglyoxal is retained by incubating with 20 mM ATP
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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
D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.661
ATP
-
isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
0.73
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1; pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
0.744
ATP
D5FLG2
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
Q4AED1, Q4AED2
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
D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.18
L-Arg
D5FLG2
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
Q4AED1, Q4AED2
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
0.26
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
0.35
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G; pH 7.9, 25°C, wild-type enzyme
0.35
L-arginine
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
0.37
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.401
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
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
O45011
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
determination of activation energy for transition state of AK reactions, thermodynamics; determination of activation energy for transition state of AK reactions, thermodynamics
-
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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
63.4
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK2
65.8
ATP
-
isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
68.3
ATP
-
isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
104
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
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
Q4AED1, Q4AED2
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