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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
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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ADP + Nomega-phospho-L-Arg
ATP + L-Arg
-
-
-
r
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
-
-
-
-
?
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 + D-Arg
ADP + Nomega-phospho-D-Arg
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
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
?
about 16% activity compared to L-Arg
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
ATP + lombricine
ADP + omega-N-phospholombricine
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
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
GDP + Nomega-phospho-L-Arg
GTP + L-Arg
-
10% of the activity with ADP
-
-
?
GTP + L-arginine
GDP + Nomega-phospho-L-arginine
UDP + Nomega-phospho-L-Arg
UTP + L-Arg
-
10% of the activity with ADP
-
-
?
additional information
?
-
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
-
no activity
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
no activity
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
D-Arg is phosphorylated to a lesser degree
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
-
D-Arg is as active as L-Arg
-
-
?
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
-
-
-
?
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
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
D5FLG2
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
McsB acts exclusively on L-Arg residues
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
highest activity
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
Isostychopus badonotus
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
Q004B5
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
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
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
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
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
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
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
strictly specific for ATP
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
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 + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
-
-
-
-
?
ATP + L-Arg

ADP + omega-N-phospho-L-Arg
-
-
-
?
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
-
-
-
?
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
O004B5
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
O004B5
-
-
-
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
-
-
-
-
?
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
-
-
-
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
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
Crassostrea sp.
-
key enzyme in invertebrate energy metabolism
-
-
?
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
Pleocyemata sp.
-
-
-
-
?
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-arginine
ADP + omega-N-phospho-L-arginine
-
-
-
-
r
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
-
-
-
-
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
-
-
-
r
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
?
-
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
?
-
-
strictly specific for ATP
-
-
-
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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15
5-guanidinopentanoic acid
-
pH 8.5, 25°C
2.796
L-arginine ethyl ester
recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
18
L-argininic acid
-
pH 8.5, 25°C
27
L-phosphocanavanine
-
37°C
0.63 - 1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
0.7 - 3.5
Nomega-phospho-L-Arg
15
octopine
-
pH 8.5, 25°C
0.192
omega-N-phospho-L-arginine
-
-
additional information
additional information
-
0.0134
ADP

-
-
0.08
ADP
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
0.14
ADP
-
mutant enzyme E314Q
0.16
ADP
-
mutant enzyme E225Q; mutant enzyme E225Q/E314Q; mutant enzyme E314S
0.23
ADP
-
wild-type enzyme
0.26
ADP
-
mutant enzyme E225D
0.284
ADP
-
isoform arginine kinase 2
0.7
ADP
-
isoform arginine kinase 1
0.023
ATP

pH 8.0, 25°C, recombinant enzyme
0.071
ATP
pH 8.0, 30°C, recombinant wild-type enzyme
0.16
ATP
pH 8.0, 25°C, recombinant enzyme
0.23
ATP
pH 7.5, 28°C, recombinant isozyme AK1
0.278
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
0.32
ATP
pH 7.5, 37°C, recombinant isozyme AK1
0.33
ATP
-
pH 8.1, mutant enzyme W208A
0.337
ATP
pH 8.0, 15°C, recombinant enzyme
0.339
ATP
pH 8.0, 17.5°C, recombinant enzyme
0.34
ATP
pH 8.0, 17.5°C, recombinant enzyme
0.35
ATP
pH 8.0, 25°C, recombinant enzyme
0.376
ATP
pH 8.0, 25°C, recombinant enzyme
0.399
ATP
pH 8.0, 20°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
0.405
ATP
pH 8.0, 22.5°C, recombinant enzyme
0.422
ATP
pH 8.0, 15°C, recombinant enzyme
0.454
ATP
pH 8.0, 30°C, recombinant enzyme
0.46
ATP
-
37°C, two-domain enzyme
0.465
ATP
pH 8.0, 20°C, recombinant enzyme
0.48
ATP
-
pH 8.1, wild-type enzyme
0.49 - 2
ATP
D5FLG2
mutant enzyme A105S, in 4.76 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
0.766
ATP
D5FLG2
mutant enzyme 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
0.8
ATP
pH 7.5, 30°C, recombinant His-tagged enzyme
0.814
ATP
-
wild-type enzyme
0.814
ATP
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.82
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G
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
0.9
ATP
pH 7.5, 30°C, recombinant His-tagged enzyme
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
0.97
ATP
-
37°C, domain 2
0.97
ATP
Crassostrea sp.
-
pH 7.9, 25°C, wild-type enzyme
0.988
ATP
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C
1.04
ATP
-
wild type enzyme
1.099
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F
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
1.132
ATP
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C
1.17
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
1.25
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
1.26
ATP
pH 8.0, 25°C, recombinant enzyme
1.27
ATP
-
pH 8.6, 30°C, recombinant arginine kinase
1.27
ATP
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
1.27
ATP
-
pH 8.0, 30°C, recombinant wild-type enzyme
1.28
ATP
-
pH 8.0, 30°C, recombinant mutant T273S
1.29
ATP
-
pH 8.6, 30°C, native arginine kinase
1.29
ATP
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
1.29
ATP
-
pH 8.0, 30°C, wild-type enzyme
1.32
ATP
-
pH 8.0, 30°C, recombinant mutant T273D
1.321
ATP
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C
1.36
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D
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
1.49
ATP
-
mutant enzyme F315Y; mutant enzyme S312R/F315H/V319E
1.59
ATP
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
1.631
ATP
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C
1.64
ATP
-
pH 8.0, 30°C, recombinant mutant T273A
1.65
ATP
-
pH 8.6, 30°C, mutant enzyme P272G
1.7
ATP
-
pH 8.0, 30°C, recombinant mutant T273G
1.93
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D/P272R
2.08
ATP
-
mutant enzyme F315H
2.17
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
2.33
ATP
purified recombinant enzyme
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
2.54
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
2.76
ATP
-
mutant enzyme F315A
2.84
ATP
-
pH 8.6, 30°C, mutant enzyme P272R
2.99
ATP
-
wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.092
ATP
-
mutant enzyme Q53A/D57A, 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
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
3.7 - 5
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
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
4.2
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F/P272G
13.3
ATP
-
mutant enzyme S282G
1.3
D-Arg

-
pH 8.5, 25°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
D-Arg
-
wild type enzyme, 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
0.106
L-Arg

D5FLG2
mutant enzyme A105S, 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
0.126
L-Arg
D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.15
L-Arg
-
pH 8.6, 25°C
0.18
L-Arg
D5FLG2
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.21
L-Arg
-
isoform arginine kinase 2
0.211
L-Arg
D5FLG2
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C
0.26
L-Arg
-
37°C, domain 2
0.37
L-Arg
-
pH 7.5, 26°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
0.42
L-Arg
-
37°C, two-domain enzyme
0.421
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C
0.52
L-Arg
-
37°C, D197G mutant enzyme of domain 2
0.52
L-Arg
-
wild type enzyme
0.578
L-Arg
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C
0.594
L-Arg
native enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
0.603
L-Arg
recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C
0.67
L-Arg
25°C, mutant enzyme D62G
0.68
L-Arg
25°C, recombinant wild-type enzyme
0.744
L-Arg
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C
0.84
L-Arg
-
mutant enzyme F315Y
0.91
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75D
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
0.95
L-Arg
-
pH 8.6, 30°C, recombinant arginine kinase
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 S312R/F315H/V319E
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
1.02
L-Arg
-
37°C, H60R mutant of domain 2
1.02
L-Arg
25°C, native enzyme
1.036
L-Arg
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C
1.13
L-Arg
-
mutant enzyme F315H
1.27
L-Arg
-
isoform arginine kinase 1
1.53
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75D/P272R
1.571
L-Arg
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C
1.74
L-Arg
25°C, native enzyme
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
2.67
L-Arg
-
mutant enzyme F315A
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
2.82
L-Arg
25°C, native enzyme
2.85
L-Arg
-
pH 8.6, 30°C, mutant enzyme P272R
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
3.45
L-Arg
25°C, mutant enzyme S63G
3.6
L-Arg
-
37°C, H60G mutant of domain 2
3.69
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C
3.78
L-Arg
-
pH 8.6, 30°C, mutant enzyme P272G
3.98
L-Arg
-
pH 8.6, 30°C, mutant enzyme Y75F/P272G
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
0.131
L-arginine
pH 8.0, 15°C, recombinant enzyme
0.165
L-arginine
pH 8.0, 20°C, recombinant enzyme
0.166
L-arginine
pH 8.0, 15°C, recombinant enzyme
0.179
L-arginine
pH 8.0, 17.5°C, recombinant enzyme
0.196
L-arginine
pH 8.0, 17.5°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
0.29
L-arginine
pH 8.0, 22.5°C, recombinant enzyme
0.3
L-arginine
pH 7.5, 30°C, recombinant His-tagged enzyme
0.3
L-arginine
pH 8.0, 20°C
0.302
L-arginine
pH 8.0, 20°C, recombinant enzyme
0.307
L-arginine
-
mutant enzyme Y89R
0.31
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
0.344
L-arginine
pH 8.0, 25°C, recombinant enzyme
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
0.35
L-arginine
pH 7.5, 30°C, recombinant His-tagged 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
0.413
L-arginine
-
wild-type enzyme
0.439
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.456
L-arginine
pH 8.0, 30°C, recombinant enzyme
0.48
L-arginine
pH 7.5, 37°C, recombinant isozyme AK1
0.538
L-arginine
pH 8.0, 30°C, recombinant enzyme
0.63
L-arginine
-
mutant enzyme H64G
0.66
L-arginine
-
pH 8.1, wild-type enzyme
0.7
L-arginine
-
pH 8.1, mutant enzyme W208A
0.779
L-arginine
pH 8.0, 35°C, recombinant enzyme
0.81
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
0.88
L-arginine
pH 8.0, 25°C, recombinant enzyme
0.912
L-arginine
wild-type two-domain enzyme
0.94
L-arginine
-
pH 8.0, 30°C, wild-type enzyme
0.95
L-arginine
-
pH 8.0, 30°C, recombinant wild-type enzyme
0.965
L-arginine
-
mutant enzyme D62G
0.98
L-arginine
-
pH 8.0, 30°C, recombinant mutant T273S
1.04
L-arginine
-
pH 8.0, 30°C, recombinant mutant T273D
1.16
L-arginine
-
mutant enzyme S282G
1.196
L-arginine
-
mutant enzyme D62_F63delinsDGF
1.44
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
1.45
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
1.46
L-arginine
-
mutant enzyme R193G
1.57
L-arginine
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
3.05
L-arginine
-
pH 8.0, 30°C, recombinant mutant T273A
3.18
L-arginine
-
pH 8.0, 30°C, recombinant mutant T273G
8.458
L-arginine
-
mutant enzyme F63G
6.7
L-canavanine

-
-
0.09
MgADP-

-
-
0.14
MgATP2-

-
-
1.4
MgATP2-
-
pH 8.5, 25°C
0.63
N5-(N-phosphonocarbamimidoyl)-L-ornithine

-
wild-type enzyme
0.68
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314D
0.72
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225D
0.88
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q
0.92
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
0.94
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
-
0.98
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314S
1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q/E314Q
0.7
Nomega-phospho-L-Arg

-
37°C
0.73
Nomega-phospho-L-Arg
-
pH 7.5, 26°C
0.74
Nomega-phospho-L-Arg
-
isoform arginine kinase 2
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
2.08
Nomega-phospho-L-Arg
-
pH 6.7, 25°C
2.1
Nomega-phospho-L-Arg
at pH 8.0 and 25°C
2.31
Nomega-phospho-L-Arg
-
isoform arginine kinase 1
3.5
Nomega-phospho-L-Arg
-
pH 7.2, 25°C
additional information
additional information

-
-
-
additional information
additional information
Pleocyemata sp.
-
-
-
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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27.3
L-(+)-(S)-canavanine
-
-
50.7
L-phosphocanavanine
-
-
0.27 - 140
N5-(N-phosphonocarbamimidoyl)-L-ornithine
0.093 - 431
Nomega-phospho-L-Arg
1.11
omega-N-phospho-L-arginine
-
pH 8, 25°C
additional information
additional information
Pleocyemata sp.
-
-
-
0.27
ADP

-
mutant enzyme E225Q/E314Q
0.34
ADP
-
mutant enzyme E225D
0.37
ADP
-
mutant enzyme E314Q
0.45
ADP
-
mutant enzyme E225Q
2.17
ADP
-
mutant enzyme E314D
116
ADP
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
140
ADP
-
wild-type enzyme
0.00229
ATP

-
mutant enzyme L65G
0.005
ATP
-
mutant enzyme E314V
0.0329
ATP
-
mutant enzyme D62_F63delinsDGF
0.443
ATP
-
mutant enzyme R193G
0.913
ATP
-
mutant enzyme D62G
3.31
ATP
-
mutant enzyme F63G
8.92
ATP
-
25°C, H60G mutant of domain 2
9.22
ATP
-
mutant enzyme Y89R
9.53
ATP
-
25°C, D197G mutant of domain 2
11.4
ATP
pH 8.0, 25°C, recombinant enzyme
18.09
ATP
-
mutant enzyme H64G
18.1
ATP
-
25°C, H60R mutant of domain 2
22.8
ATP
-
mutant enzyme S282G
22.9
ATP
wild-type two-domain enzyme
24.4
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G/K193G
25.3
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62G
25.7
ATP
-
wild-type enzyme
32.4
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193G
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
38.9
ATP
-
pH 7.5, 25°C, recombinant enzyme
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
40.8
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme K193R
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
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D
41.9
ATP
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
42.1
ATP
Crassostrea sp.
-
pH 7.9, 25°C, mutant enzyme N62D/K193R
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
44.7
ATP
-
25°C, domain 2
45
ATP
pH 8.0, 25°C, recombinant enzyme
47.5
ATP
Crassostrea sp.
-
pH 7.9, 25°C, wild-type enzyme
50.1
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
54.16
ATP
-
pH 8.0, 30°C, recombinant mutant T273G
60.3
ATP
-
pH 8.6, 30°C, mutant enzyme P272R
60.7
ATP
-
isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C
60.97
ATP
-
pH 8.0, 30°C, recombinant mutant T273A
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
73.3
ATP
-
25°C, two-domain enzyme
74.6
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F/P272G
79.2
ATP
-
pH 8.6, 30°C, mutant enzyme P272G
88
ATP
pH 8.0, 30°C, recombinant wild-type enzyme
104
ATP
pH 8.0, 25°C, recombinant His6-tagged isozyme AK1
126.2
ATP
-
pH 8.6, 30°C, mutant enzyme Y75F
129
ATP
recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains
140.7
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D
141.3
ATP
-
pH 8.6, 30°C, mutant enzyme Y75D/P272R
143.2
ATP
-
pH 8.0, 30°C, recombinant mutant T273D
151.3
ATP
-
pH 8.0, 30°C, recombinant mutant T273S
159.4
ATP
-
pH 8.6, 30°C, recombinant arginine kinase
159.4
ATP
-
pH 8.0, 30°C, recombinant wild-type enzyme
163
ATP
-
pH 8.6, 30°C, native arginine kinase
163
ATP
-
pH 8.0, 30°C, wild-type enzyme
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