Information on EC 2.7.3.3 - arginine kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.3.3
-
RECOMMENDED NAME
GeneOntology No.
arginine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
show the reaction diagram
rapid equilibrium random mechanism
-
ATP + L-arginine = ADP + Nomega-phospho-L-arginine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-arginine Nomega-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosine 5'-triphosphate-arginine phosphotransferase
-
-
-
-
adenosine 5'-triphosphate: L-arginine phosphotransferase
-
-
-
-
AK
-
-
-
-
AK: L-arginine phosphotransferase
-
-
arginine kinase 1
Q4AED2
-
arginine kinase 2
Q4AED1
-
arginine kinase-1
E2JE77
-
arginine phosphokinase
-
-
-
-
ArgK
-
-
-
-
ark
Q1DA50
-
ark
Myxococcus xanthus DK1622
Q1DA50
-
-
ATP: arginine N-phosphotransferase
-
-
ATP: arginine N-phosphotransferase
B0FRF9
-
ATP: arginine phosphotransferase
-
-
ATP: L-arginine phosphototransferase
Q4KY22
-
ATP: L-arginine phosphotransferase
-
-
ATP: L-arginine phosphotransferase
Q2F5T5
-
ATP: L-arginine phosphotransferase
-
-
ATP: L-arginine phosphotransferase
P51541
-
ATP: L-arginine phosphotransferase
-
-
ATP: L-arginine phosphotransferase
A6M9J4
-
ATP: L-arginine phosphotransferase
B1PVZ9
-
ATP:arginine N-phosphotransferase
-
-
ATP:arginine phosphotransferase
-
-
ATP:arginine phosphotransferase
Phytomonas sp. Jma
-
-
-
ATP:L-arginine N-phosphotransferase
-
-
-
-
ATP:L-arginine N-phosphotransferase
-
-
ATP:L-arginine N-phosphotransferase
-
-
ATP:L-arginine omega-N-phosphotransferase
H9BZ68
-
ATP:L-arginine phosphotransferase
-
-
ATP:L-arginine phosphotransferase
-
-
ATP:L-arginine phosphotransferase
A6M9J4
-
ATP:L-arginine phosphotransferase
-
-
kinase, arginine (phosphorylating)
-
-
-
-
MXAN2252 protein
Q1DA50
-
MXAN2252 protein
Myxococcus xanthus DK1622
Q1DA50
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-70-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
three isoforms transcribed from a single gene: a, b, and c
Uniprot
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
B3TNF8
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
lines NB, 306 and BC8
UniProt
Manually annotated by BRENDA team
silkworm
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Crassostrea sp.
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Southern pink shrimp
-
-
Manually annotated by BRENDA team
Chinese shrimp
-
-
Manually annotated by BRENDA team
fleshy prawn
Q4KY22
UniProt
Manually annotated by BRENDA team
Indian white prawn
-
-
Manually annotated by BRENDA team
Isostychopus badonotus
sea cucumber
-
-
Manually annotated by BRENDA team
atlantic horseshoe crab
-
-
Manually annotated by BRENDA team
Pacific white shrimp
-
-
Manually annotated by BRENDA team
fragment
B3TNE4
SwissProt
Manually annotated by BRENDA team
Australian sheep blowfly
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Greasyback shrimp
UniProt
Manually annotated by BRENDA team
Greasyback shrimp
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Myxococcus xanthus DK1622
-
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Northern shrimp
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
giant tiger prawn
-
-
Manually annotated by BRENDA team
Phytomonas sp. Jma
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Pleocyemata sp.
-
-
-
Manually annotated by BRENDA team
Argentine red shrimp
-
-
Manually annotated by BRENDA team
Portunus sp.
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
mud crab
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
B0FRF9
arginine kinase may play an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
Q2F5T5
arginine kinase is involved in the antiviral process of Bombyx mori larvae against nucleopolyhedrovirus infection
physiological function
E2JE77, -
the enzyme plays an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
-, Q1DA50
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
physiological function
Myxococcus xanthus DK1622
-
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
-
the enzyme is a modulator of energetic reserves under starvation stress conditions, activity is post-transcriptionally regulated
-
-
-
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
-, 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-Arg
show the reaction diagram
H9BZ68
-
-
-
r
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
show the reaction diagram
-
-
-
-
?
ADP + omega-N-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
A4F2K7, -
function: five residues predicted to interact with the substrate arginine (S77, Y82, E239, C285 and E328), and five residues predicted to interact with the substrate ADP (R138, R140, R243, R294 and R323). Arginine (or phosphagen) and MgATP (or MgADP), typically exhibit synergistic binding to arginine kinase
-
-
r
ATP + 4-guanidinebutanoic acid
ADP + N-phospho-4-guanidinobutanoic acid
show the reaction diagram
-
8% of the activity with L-Arg
-
-
?
ATP + 5-guanidinopentanoic acid
ADP + N-phospho-5-guanidinopentanoic acid
show the reaction diagram
-
10% of the activity with L-Arg
-
-
?
ATP + CtsR-L-Arg
ATP + CtsR-N-phospho-L-Arg
show the reaction diagram
-
McsB specifically phosphorylates arginine residues in the DNA binding domain of CtsR, thereby impairing its function as a repressor of stress response genes, phosphorylation of CtsR by McsB is sufficient to inhibit the repressor function of CtsR
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
-
no activity
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
-
no activity
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
-
D-Arg is as active as L-Arg
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
-
D-Arg is phosphorylated to a lesser degree
-
-
-
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
35.2% relative activity compared to L-Arg
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
35.2% of the activity with L-Arg
-
-
?
ATP + D-Arg
ADP + Nomega-phospho-D-Arg
show the reaction diagram
-
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
show the reaction diagram
Q4AED1, Q4AED2, -
-
-
-
?
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
7.6% of the activity with L-Arg
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
O96507
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, O61367
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
P51541
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, Q004B5
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
-
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, Q9NKV6
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, Q9NKV5
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Q9NKV4, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
A7YVI5, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
A4F2K7, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
A6M9J4, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Isostychopus badonotus
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
B1PVZ9
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
B0FRF9
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, Q2F5T5
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Q2F5T5
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, Q1DA50
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-, D5FLG2
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Q4KY22
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
E2JE77, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
highest activity
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
100% activity
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
strictly specific for ATP
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
the enzyme is involved in the storage of the high-energy phosphate reserve phosphoarginine
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
production of high-energy reserves N-phospho-L-Arg in insect muscles
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
McsB acts exclusively on L-Arg residues
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
isoforms AK1 and AK2 are primarily active towards L-arginine
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
H9BZ68
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
show the reaction diagram
Phytomonas sp. Jma
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
Myxococcus xanthus DK1622
Q1DA50
-
-
-
r
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
O15992
-
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
-
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
-, Q004B5
arginine kinase is an allergenic protein
-
-
?
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
A7YVI5, -
synergism for substrate binding
-
-
r
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
-
synergism in substrate binding
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
-
-
-
-
r
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
show the reaction diagram
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
show the reaction diagram
Pleocyemata sp.
-
-
-
-
?
ATP + L-arginine
ADP + Nomega-phosphono-L-arginine
show the reaction diagram
Crassostrea sp.
-
key enzyme in invertebrate energy metabolism
-
-
?
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
show the reaction diagram
-
-
-
-
r
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
show the reaction diagram
-
-
-
-
r
ATP + L-arginine
ADP + omega-N-phospho-L-arginine
show the reaction diagram
-, Q4AEC4
both domains of Calyptogena arginine kinase are catalytically competent, although domain 2 strongly influences catalysis in domain 1
-
-
r
ATP + L-arginine ethyl ester
ADP + Nomega-phospho-L-Arg ethyl ester
show the reaction diagram
H9BZ68
6% activity compared to L-Arg
-
-
?
ATP + L-arginine methyl ester
ADP + Nomega-phospho-L-arginine methyl ester
show the reaction diagram
-
-
-
-
?
ATP + L-arginine-O-ethyl ester
?
show the reaction diagram
-
isoform arginine kinase 2 shows about 16% activity of that obtained with L-Arg
-
-
?
ATP + L-argininic acid
ADP + Nomega-phospho-L-argininic acid
show the reaction diagram
-
45% of the activity with L-Arg
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
show the reaction diagram
-
-
-
r
ATP + L-canavanine
ADP + L-phosphocanavanine
show the reaction diagram
-
7% of the activity with L-Arg
-
-
r
ATP + L-canavanine
ADP + L-phosphocanavanine
show the reaction diagram
-
7.3% of the activity with L-Arg
-
-
r
ATP + L-canavanine
ADP + L-phosphocanavanine
show the reaction diagram
-
L-canavanine is a weak substrate
-
-
?
ATP + L-canavanine
ADP + L-phosphocanavanine
show the reaction diagram
-
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
?
show the reaction diagram
H9BZ68
about 16% activity compared to L-Arg
-
-
?
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
show the reaction diagram
-
25% of the activity with L-Arg
-
-
?
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
show the reaction diagram
-
isoform arginine kinase 2 shows about 37% activity of that obtained with L-Arg
-
-
?
ATP + L-homoarginine
ADP + Nomega-phospho-L-homoarginine
show the reaction diagram
H9BZ68
7% activity compared to L-Arg
-
-
?
ATP + lombricine
ADP + omega-N-phospholombricine
show the reaction diagram
Q4AED1, Q4AED2, -
0.17% of the activity with L-Arg
-
-
?
ATP + lombricine
ADP + omega-N-phospholombricine
show the reaction diagram
Q4AED1, Q4AED2, -
3.0% of the activity with L-Arg
-
-
?
ATP + N-acetyl-L-Arg
ADP + Nomega-phospho-N-alpha-acetyl-L-Arg
show the reaction diagram
-
13% of the activity with L-Arg
-
-
?
ATP + octopine
ADP + N-phospho-D-octopine
show the reaction diagram
-
30% of the activity with L-Arg
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AED1, Q4AED2, -
0.11% of the activity with L-Arg
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AED1, Q4AED2, -
2.7% of the activity with L-Arg
-
-
?
UDP + Nomega-phospho-L-Arg
UTP + L-Arg
show the reaction diagram
-
10% of the activity with ADP
-
-
?
GDP + Nomega-phospho-L-Arg
GTP + L-Arg
show the reaction diagram
-
10% of the activity with ADP
-
-
?
additional information
?
-
-
strictly specific for ATP
-
-
-
additional information
?
-
A7YVI5, -
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
?
-
-
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
?
-
-, D5FLG2
no activity towards D-arginine, creatine, glycocyamine, and taurocyamine
-
-
-
additional information
?
-
H9BZ68
no activity with D-arginine, N-acetyl-L-arginine, agmatine, and creatine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
-
the enzyme is a modulator of energetic reserves under starvation stress conditions, activity is post-transcriptionally regulated
-
-
-
ADP + Nomega-phospho-L-Arg
ATP + L-arginine
show the reaction diagram
-, O61367
the enzyme is an important component of the energy releasing mechanism in the visual system that has high and fluctuating energy demands
-
-
?
ATP + D-Arg
ADP + omega-N-phospho-D-Arg
show the reaction diagram
Q4AED1, Q4AED2, -
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
the enzyme is involved in the storage of the high-energy phosphate reserve phosphoarginine
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
production of high-energy reserves N-phospho-L-Arg in insect muscles
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
4% of the activation with Mg2+
Ca2+
-
activates
Ca2+
-
4 mM, 19% of the activation with Mg2+
Ca2+
-
less effactive than Mg2+ in activation
Ca2+
-
a divalent cation such as Mg2+, Mn2+ or Ca2+ is required
Ca2+
-
activates
Co2+
-
activates
Co2+
-
4 mM, 26% of the activation with Mg2+
Cu2+
-
activates
Fe2+
-
4 mM, 12% of the activation with 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+
-
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
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+
-
5-10 mM required
Mg2+
-
4 mM, activation
Mg2+
-
required
Mg2+
-
most effective divalent cation for activation
Mg2+
-
required, Km-value: 0.476 mM, formation of ATP
Mg2+
-
a divalent cation such as Mg2+, Mn2+ or Ca2+ is required
Mg2+
-
activates at concentrations greater than 1 mM, maximal effect at 1.5 mM
Mg2+
-
required in complex with ATP
Mg2+
B0FRF9
required
Mg2+
-
required, bound to ATP
Mn2+
-
4 mM, activation; less 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
Mn2+
-
4 mM, activation; less effective than Mg2+ in activation
Mn2+
-
less effective than Mg2+ in activation
Mn2+
-
less effective than Mg2+ in activation; more effective than Mg2+ in activation
Mn2+
-
less effective than Mg2+ in activation
Mn2+
-
less effective than Mg2+ in activation
Mn2+
-
a divalent cation such as Mg2+, Mn2+ or Ca2+ is required
Sn2+
-
4 mM, 13% of the activation with Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
B0FRF9
the enzyme activity is inhibited by 10 mM 2-oxoglutarate
2-oxoglutarate
E2JE77, -
the enzyme activity is inhibited at 10-200 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis-(2-nitrobenzoic acid)
-
modification and inactivation course with DTNB and the reactivation course of DTNB-modified enzyme. Modified enzyme can be reactivated by an excess concentration of dithiothreitol in a monophasic kinetic course
5,5'-dithiobis-2-nitrobenzoic acid
-
-
Ag+
-
dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+
agmatine
-
5fold higher concentration than L-Arg, 20% inhibition
agmatine
-
10 mM, 79.3% inhibition
Aminoguanidine
-
10 mM, 2.6% inhibition
aspartate
-
0.02-0.15 mM, causes inactivation and unfolding of arginine kinase
ATP
-
product inhibition, competitive with ADP, noncompetitive with L-Arg
ATP
B0FRF9
the enzyme is inhibited by 200 mM ATP
ATP
E2JE77, -
the enzyme activity is inhibited at 100 mM
canavanine
-
5fold higher concentration than L-Arg, 50% inhibition
canavanine
-
10 mM, 54.6% inhibition
chloride
Isostychopus badonotus
-
9% inhibition at 50 mM
chloride
-
7% inhibition at 50 mM
chloride
-
50 mM, 7% inhibition
Creatine
-
10 mM, 12.7% inhibition
Cu2+
-
strong inhibition
D-Arg
-
product inhibition, competitive with arginine phosphate and noncompetitive withg ADP
D-Arg
-
competitive to L-arginine
D-Arginine
-
competitive
D-glucose
B0FRF9
the enzyme is inhibited by 50 mM D-glucose, almost all arginine kinase activity is lost after treatment with 200 mM D-glucose
dithiothreitol
-
conformational change and inactivation
DTNB
-
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course. This reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site
Ethylguanidine
-
5fold higher concentration than L-Arg, 22% inhibition
guanidine butyrate
-
10 mM, 4.3% inhibition
guanidine hydrochloride
-
0.2 mM, about 90% loss of activity
guanidine hydrochloride
-
1 mM
His
-
5fold higher concentration than L-Arg, 50% inhibition
Homoarginine
-
10 mM, 38.2% inhibition
Iodide
Isostychopus badonotus
-
13% inhibition at 50 mM
Iodide
-
3% inhibition at 50 mM
Iodide
-
50 mM, 3% inhibition
iodoacetamide
-
-
K+
-
200 mM, 50% inhibition
L-arginine methyl ester
-
competitive to L-Arg
L-Asp
-
5fold higher concentration than L-Arg, 25% inhibition
L-canavanine
-
competitive to L-Arg
L-canavanine
-
-
L-Glu
-
5fold higher concentration than L-Arg, 31% inhibition
L-Glucose
E2JE77, -
AK-1 activity does not show significant variation after supplementation with 10 mM L-glucose. However, AK-1 activity decreases significantly when L-glucose concentration is higher than 50 mM and almost all MrAK-1 activity is lost after treatment with 200 mM L-glucose
L-histidine
-
10 mM, 2.4% inhibition
L-Homoarginine
-
5fold higher concentration than L-Arg, 33% inhibition
L-Lys
-
5fold higher concentration than L-Arg, 25% inhibition
L-nitroarginine
-
5fold higher concentration than L-Arg, 28% inhibition
L-nitroarginine
-
10 mM, 52.6% inhibition
Mg2+
-
at high concentrations noncompetitive inhibition of MgATP2-
MgADP-
-
inhibition is potentiated by NO3-
MgATP2-
-
enzyme form AK2 is strongly inhibited at high concentrations
N-methyl-L-Arg
-
5fold higher concentration than L-Arg, 28% inhibition
Na+
-
200 mM, 50% inhibition
NH4+
-
200 mM, 50% inhibition
nitrate
Isostychopus badonotus
-
88% inhibition at 50 mM
-
nitrate
-
99% inhibition at 50 mM
-
nitrate
-
50 mM, 99% inhibition
-
nitrite
Isostychopus badonotus
-
76% inhibition at 50 mM
nitrite
-
96% inhibition at 50 mM
nitrite
-
50 mM, 96% inhibition
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal
rutin
-
noncompetitive inhibitor, i.e. 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxymethyl]oxan-2-yl]oxychromen-4-one, about 20% residual activity at 0.02-0.06 mM rutin
Thiocyanate
Isostychopus badonotus
-
16% inhibition at 50 mM
Thiocyanate
-
21% inhibition at 50 mM
Thiocyanate
-
50 mM, 21% inhibition
Zn2+
-
strong inhibition
Mn2+
-
at high concentrations noncompetitive inhibition of MgATP2-
additional information
-
not inhibited by 50 mM acetate
-
additional information
B0FRF9
arginine kinase activity does not show significant variation after incubated with 10-200 mM L-citrulline, L-ornaline, and glycerol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetate
Isostychopus badonotus
-
5.5% activation at 50 mM
ATP
-
about 80% of the activity formerly inhibited by phenylglyoxal is retained by incubating with 20 mM ATP
ATP
B0FRF9
after treatment with 10 mM ATP, the enzyme activity significantly increases
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
nifurtimox
-
produces 2.3fold increase in enzyme expression at 0.01 mM
proline
-
with proline the residual activity of AK after incubation in guanidine hydrochloride is higher than without proline
Sucrose
-
maintains the activity of the enzyme in the presence of guanidine hydrochloride
hydrogen peroxide
-
produces up to 10fold increase in enzyme expression at 0.2 mM
additional information
-
not affected by sodium nitroprusside, methylene blue and benznidazole
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15
-
5-guanidinopentanoic acid
-
pH 8.5, 25C
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
0.2
-
ADP
-
pH 7.2, 25C
0.23
-
ADP
-
wild-type enzyme
0.26
-
ADP
-
mutant enzyme E225D
0.284
-
ADP
-
isoform arginine kinase 2
0.42
-
ADP
-
pH 7.5, 26C
0.7
-
ADP
-
isoform arginine kinase 1
1.25
-
ADP
-
pH 6.7, 25C
0.3
-
ATP
-
30C, pH 7.3
0.3
-
ATP
A7YVI5, -
; in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25C
0.33
-
ATP
-
pH 8.1, mutant enzyme W208A
0.4
-
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
0.46
-
ATP
-
37C, two-domain 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 25C
0.654
-
ATP
-, D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25C
0.661
-
ATP
-
isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
0.744
-
ATP
-, D5FLG2
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
0.766
-
ATP
-, D5FLG2
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
0.774
-
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
0.8
-
ATP
-
pH 7.6, 25C
0.814
-
ATP
-
wild-type enzyme
0.814
-
ATP
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
0.82
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G
0.823
-
ATP
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
0.837
-
ATP
-
isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
0.926
-
ATP
-
isoform AK2 mutant G54S, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
0.93
-
ATP
-
isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
0.95
-
ATP
A4F2K7, -
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25C; pH 8, 25C
0.97
-
ATP
-
37C, domain 2
0.97
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, wild-type enzyme
0.988
-
ATP
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30C
1.01
-
ATP
-
at 25C
1.04
-
ATP
-
wild type enzyme
1.099
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75F
1.12
-
ATP
-
isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
1.13
-
ATP
-
wild type enzyme isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
1.132
-
ATP
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30C
1.17
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D
1.25
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193R
1.27
-
ATP
-
pH 8.6, 30C, recombinant arginine kinase
1.27
-
ATP
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
1.29
-
ATP
-
pH 8.6, 30C, native arginine kinase
1.29
-
ATP
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
1.321
-
ATP
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30C
1.36
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75D
1.36
-
ATP
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30C
1.42
-
ATP
-
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30C
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 25C
1.631
-
ATP
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30C
1.65
-
ATP
-
pH 8.6, 30C, mutant enzyme P272G
1.93
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75D/P272R
2.08
-
ATP
-
mutant enzyme F315H
2.17
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193G
2.33
-
ATP
B1PVZ9
purified recombinant enzyme
2.35
-
ATP
-
pH 7.5, 26C
2.38
-
ATP
-
mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30C
2.42
-
ATP
-
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30C
2.54
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D/K193R
2.76
-
ATP
-
mutant enzyme F315A
2.84
-
ATP
-
pH 8.6, 30C, 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 25C
3.092
-
ATP
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30C
3.49
-
ATP
-
isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
3.56
-
ATP
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30C
3.68
-
ATP
-
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30C
3.7
5
ATP
Crassostrea sp.
-
pH 7.9, 25C, 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 25C
4.06
-
ATP
-
mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30C
4.15
-
ATP
-
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30C
4.2
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75F/P272G
13.3
-
ATP
-
mutant enzyme S282G
1.3
-
D-Arg
-
pH 8.5, 25C
3.14
-
D-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25C
4.4
-
D-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25C
6.45
-
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25C
9
-
D-Arg
-
wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25C
9.34
-
D-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25C
9.55
-
D-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25C
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 25C
0.106
-
L-Arg
-, D5FLG2
mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25C
0.12
-
L-Arg
A7YVI5, -
; in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25C
0.126
-
L-Arg
-, D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25C
0.15
-
L-Arg
-
pH 8.6, 25C
0.18
-
L-Arg
-, D5FLG2
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
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 25C
0.26
-
L-Arg
-
37C, domain 2
0.3
-
L-Arg
-
30C, pH 7.3
0.37
-
L-Arg
-
pH 7.5, 26C
0.389
-
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25C
0.413
-
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
0.42
-
L-Arg
-
37C, two-domain enzyme
0.421
-
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
0.5
-
L-Arg
-
7C
0.52
-
L-Arg
-
37C, D197G mutant enzyme of domain 2
0.52
-
L-Arg
-
at 25C
0.52
-
L-Arg
-
wild type enzyme
0.578
-
L-Arg
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30C
0.594
-
L-Arg
H9BZ68
native enzyme, in 50 mM TrisHCl pH 7.5, at 22C
0.603
-
L-Arg
H9BZ68
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22C
0.67
-
L-Arg
-, Q9NKV6
-
0.67
-
L-Arg
-, Q9NKV5
25C, mutant enzyme D62G
0.68
-
L-Arg
-, Q9NKV6
-
0.68
-
L-Arg
-, Q9NKV5
25C, recombinant wild-type enzyme
0.744
-
L-Arg
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30C
0.8
-
L-Arg
-
pH 8.5, 25C
0.84
-
L-Arg
-
mutant enzyme F315Y
0.91
-
L-Arg
-
pH 8.6, 30C, mutant enzyme Y75D
0.94
-
L-Arg
-
pH 8.6, 30C, mutant enzyme Y75F; pH 8.6, 30C, native arginine kinase
0.94
-
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
0.95
-
L-Arg
-
pH 8.6, 30C, recombinant arginine kinase
0.951
-
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
0.98
-
L-Arg
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30C
0.99
-
L-Arg
-
mutant enzyme S312R/F315H/V319E
0.99
-
L-Arg
-
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30C
1
-
L-Arg
-
pH 7.6, 25C
1.01
-
L-Arg
A4F2K7, -
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25C; pH 8, 25C
1.02
-
L-Arg
-
37C, H60R mutant of domain 2
1.02
-
L-Arg
-, Q9NKV6
25C, native enzyme
1.036
-
L-Arg
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30C
1.13
-
L-Arg
-
mutant enzyme F315H
1.27
-
L-Arg
-
isoform arginine kinase 1
1.35
-
L-Arg
-
-
1.53
-
L-Arg
-
pH 8.6, 30C, mutant enzyme Y75D/P272R
1.571
-
L-Arg
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30C
1.59
-
L-Arg
B1PVZ9
-
1.74
-
L-Arg
Q9NKV4, -
25C, native enzyme
1.74
-
L-Arg
-
mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30C
1.81
-
L-Arg
-
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30C
2.05
-
L-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25C
2.5
3
L-Arg
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30C
2.67
-
L-Arg
-
mutant enzyme F315A
2.72
-
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25C
2.726
-
L-Arg
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30C
2.82
-
L-Arg
-, Q9NKV5
25C, native enzyme
2.85
-
L-Arg
-
pH 8.6, 30C, mutant enzyme P272R
2.98
-
L-Arg
-
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30C
3.04
-
L-Arg
-
mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30C
3.25
-
L-Arg
-
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30C
3.45
-
L-Arg
-, Q9NKV6
-
3.45
-
L-Arg
-, Q9NKV5
25C, mutant enzyme S63G
3.6
-
L-Arg
-
37C, H60G mutant of domain 2
3.69
-
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25C
3.78
-
L-Arg
-
pH 8.6, 30C, mutant enzyme P272G
3.98
-
L-Arg
-
pH 8.6, 30C, mutant enzyme Y75F/P272G
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 25C
5.07
-
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25C
6.45
-
L-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25C
34.3
-
L-Arg
Q4AED1, Q4AED2, -
25C
35.4
-
L-Arg
Q4AED1, Q4AED2, -
25C
18
-
L-arginic acid
-
pH 8.5, 25C
-
0.307
-
L-arginine
-
mutant enzyme Y89R
0.31
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D
0.35
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G; pH 7.9, 25C, wild-type enzyme
0.413
-
L-arginine
-
wild-type enzyme
0.49
-
L-arginine
-
-
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
0.81
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D/K193R
0.912
-
L-arginine
-, Q4AEC4
wild-type two-domain enzyme
0.965
-
L-arginine
-
mutant enzyme D62G
1.16
-
L-arginine
-
mutant enzyme S282G
1.196
-
L-arginine
-
mutant enzyme D62_F63delinsDGF
1.44
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G/K193G
1.45
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193G
1.46
-
L-arginine
-
mutant enzyme R193G
1.57
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193R
8.458
-
L-arginine
-
mutant enzyme F63G
2.796
-
L-arginine ethyl ester
H9BZ68
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22C
-
6.7
-
L-canavanine
-
-
22
-
L-canavanine
-
37C
27
-
L-phosphocanavanine
-
37C
0.45
-
MgADP-
-
37C
1.3
-
MgATP2-
-
-
30
-
N-acetyl-L-Arg
-
-
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
-
37C
0.73
-
Nomega-phospho-L-Arg
-
pH 7.5, 26C
0.74
-
Nomega-phospho-L-Arg
-
isoform arginine kinase 2
1.166
-
Nomega-phospho-L-Arg
H9BZ68
native enzyme, in 50 mM TrisHCl pH 7.5, at 22C
1.432
-
Nomega-phospho-L-Arg
H9BZ68
recombinant enzyme, in 50 mM TrisHCl pH 7.5, at 22C
2.08
-
Nomega-phospho-L-Arg
-
pH 6.7, 25C
2.1
-
Nomega-phospho-L-Arg
-, Q1DA50
at pH 8.0 and 25C
2.31
-
Nomega-phospho-L-Arg
-
isoform arginine kinase 1
3.5
-
Nomega-phospho-L-Arg
-
pH 7.2, 25C
15
-
octopine
-
pH 8.5, 25C
0.192
-
omega-N-phospho-L-arginine
-
-
1.4
-
MgATP2-
-
pH 8.5, 25C
additional information
-
additional information
-
-
-
additional information
-
additional information
Pleocyemata sp.
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
1.11
-
ADP
-
pH 8, 25C
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
2.02
-
ATP
A4F2K7, -
pH 8, 25C
3.31
-
ATP
-
mutant enzyme F63G
8.92
-
ATP
-
25C, H60G mutant of domain 2
9.22
-
ATP
-
mutant enzyme Y89R
9.53
-
ATP
-
25C, D197G mutant of domain 2
18.09
-
ATP
-
mutant enzyme H64G
18.1
-
ATP
-
25C, H60R mutant of domain 2
22.8
-
ATP
-
mutant enzyme S282G
22.9
-
ATP
-, Q4AEC4
wild-type two-domain enzyme
24.4
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G/K193G
25.3
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G
25.7
-
ATP
-
wild-type enzyme
29.18
-
ATP
A7YVI5, -
-
32.4
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193G
33.4
-
ATP
-
isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
36.6
-
ATP
-
wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
39.5
-
ATP
-
wild type isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
40.8
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193R
41
-
ATP
-
isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
41.9
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D
41.9
-
ATP
-
isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
42.1
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, 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 25C
43.3
-
ATP
-
isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
44.7
-
ATP
-
25C, domain 2
47.5
-
ATP
Crassostrea sp.
-
pH 7.9, 25C, wild-type enzyme
50.1
-
ATP
-
isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
60.3
-
ATP
-
pH 8.6, 30C, mutant enzyme P272R
60.7
-
ATP
-
isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
61.8
-
ATP
-
isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
65.8
-
ATP
-
isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
68.3
-
ATP
-
isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25C
73.3
-
ATP
-
25C, two-domain enzyme
74.6
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75F/P272G
79.2
-
ATP
-
pH 8.6, 30C, mutant enzyme P272G
126.2
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75F
129
-
ATP
O15992
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, 30C, mutant enzyme Y75D
141.3
-
ATP
-
pH 8.6, 30C, mutant enzyme Y75D/P272R
159.4
-
ATP
-
pH 8.6, 30C, recombinant arginine kinase
163
-
ATP
-
pH 8.6, 30C, native arginine kinase
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 25C
40.8
-
D-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25C
61.5
-
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25C
86.7
-
D-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25C
90.7
-
D-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25C; isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25C
121
-
D-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25C
0.08
-
L-Arg
-
mutant enzyme S312G/E314V/F315D/E317A/S318A/G321S
0.833
-
L-Arg
-
mutant enzyme F315Y
1.02
-
L-Arg
-
mutant enzyme F315A
1.1
-
L-Arg
-
wild type enzyme
2.02
-
L-Arg
A4F2K7, -
in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25C; pH 8, 25C
2.73
-
L-Arg
-
two-domain enzyme, in 100 mM Tris-HCl (pH 8.0), at 10C
3.97
-
L-Arg
-
mutant enzyme F315H
4.3
-
L-Arg
-
two-domain enzyme, in 100 mM Tris-HCl (pH 8.0), at 25C
4.38
-
L-Arg
-
mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30C
5.54
-
L-Arg
-
mutant enzyme S312R/F315H/V319E
5.8
-
L-Arg
Q4AED1, Q4AED2, -
25C; 25C
7.4
-
L-Arg
-
isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 10C
8.92
-
L-Arg
-
25C, H60G mutant of domain 2
9.53
-
L-Arg
-
25C, D197G mutant of domain 2
10.26
-
L-Arg
-
mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30C
13.09
-
L-Arg
-
mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30C
13.7
-
L-Arg
-
isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 25C
15.67
-
L-Arg
-
mutant enzyme F315Y
15.95
-
L-Arg
-
mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30C
18.1
-
L-Arg
-
25C, H60R mutant of domain 2
18.66
-
L-Arg
-
wild type enzyme
23.33
-
L-Arg
-
mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30C
25.7
-
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
29.18
-
L-Arg
A7YVI5, -
-
29.93
-
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
34.8
-
L-Arg
-, D5FLG2
mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25C
35.4
-
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 25C
43.3
-
L-Arg
-, D5FLG2
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
44.7
-
L-Arg
-
25C, domain 2
45.1
-
L-Arg
-, D5FLG2
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
45.9
-
L-Arg
-, D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25C
46
-
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25C
56.21
-
L-Arg
-
mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30C
60.36
-
L-Arg
-
mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30C
62.3
-
L-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25C
64.43
-
L-Arg
-
mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30C
70.93
-
L-Arg
-
mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30C
73.3
-
L-Arg
-
25C, two-domain enzyme
75.4
-
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25C
77.8
-
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25C
81
-
L-Arg
A7YVI5, -
in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25C
81.2
-
L-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25C
89
-
L-Arg
-
mutant two-domain-enzyme D1(Y68G)-D2, in 100 mM Tris/HCl, pH 8.0 at 25C
104
-
L-Arg
-
wild type one-domain-enzyme D1, in 100 mM Tris/HCl, pH 8.0 at 25C
105.6
-
L-Arg
-
mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30C
109.8
-
L-Arg
-
mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30C
121
-
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25C
123
-
L-Arg
-
mutant two-domain-enzyme D1-D2(Y68G), in 100 mM Tris/HCl, pH 8.0 at 25C
129
-
L-Arg
O15992
recombinant wild-type enzyme with MBP tag
139
-
L-Arg
-
-
151.2
-
L-Arg
-
mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30C
152.2
-
L-Arg
-
mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30C
157
-
L-Arg
-
wild type one-domain-enzyme D2, in 100 mM Tris/HCl, pH 8.0 at 25C
159.4
-
L-Arg
-
recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
163
-
L-Arg
-
native wild type enzyme, in 100 mM Tris, pH 8.0, at 30C
187
-
L-Arg
-
mutant two-domain-enzyme D1-Lys6-D2, in 100 mM Tris/HCl, pH 8.0 at 25C
678
-
L-Arg
-
wild type two-domain-enzyme D1-D2, in 100 mM Tris/HCl, pH 8.0 at 25C
0.00229
-
L-arginine
-
mutant enzyme L65G
0.005
-
L-arginine
-
mutant enzyme E314V
0.0329
-
L-arginine
-
mutant enzyme D62_F63delinsDGF
0.443
-
L-arginine
-
mutant enzyme R193G
0.913
-
L-arginine
-
mutant enzyme D62G
3.31
-
L-arginine
-
mutant enzyme F63G
9.22
-
L-arginine
-
mutant enzyme Y89R
18.09
-
L-arginine
-
mutant enzyme H64G
22.8
-
L-arginine
-
mutant enzyme S282G
24.4
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G/K193G
25.3
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62G
25.7
-
L-arginine
-
wild-type enzyme
32.4
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193G
40.8
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme K193R
41.9
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D
42.1
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, mutant enzyme N62D/K193R
47.5
-
L-arginine
Crassostrea sp.
-
pH 7.9, 25C, wild-type enzyme
212.9
-
L-arginine
-, Q4AEC4
wild-type two-domain enzyme
27.3
-
L-canvanine
-
-
-
0.27
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q/E314Q
0.34
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225D
0.37
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314D
0.45
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E225Q
2.17
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme E314S
116
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
mutant enzyme R312G/E314V/H315D/E317A/E319V
140
-
N5-(N-phosphonocarbamimidoyl)-L-ornithine
-
wild-type enzyme
0.093
-
Nomega-phospho-L-Arg
-, Q1DA50
at pH 8.0 and 25C
431
-
Nomega-phospho-L-Arg
-
-
1.11
-
omega-N-phospho-L-arginine
-
pH 8, 25C
50.7
-
L-phosphocanavanine
-
-
additional information
-
additional information
Pleocyemata sp.
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.52
-
D-Arg
-
wild type enzyme, in 100 mM Tris/HCl (pH 8.0), at 25C
9101
9.29
-
D-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25C
9101
9.52
-
D-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25C
9101
9.54
-
D-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25C
9101
27.5
-
D-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25C
9101
29
-
D-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25C
9101
9.65
-
L-Arg
-
isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25C
12085
12.5
-
L-Arg
-
wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25C
12085
15.4
-
L-Arg
-
isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25C
12085
39.5
-
L-Arg
-
isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25C
12085
44.7
-
L-Arg
-
isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25C
12085
195
-
L-Arg
-
isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25C
12085
215
-
L-Arg
-, D5FLG2
mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
12085
241
-
L-Arg
-, D5FLG2
mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25C
12085
316
-
L-Arg
-, D5FLG2
mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25C
12085
352
-
L-Arg
-, D5FLG2
recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25C
12085
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0028
-
Ag+
-
at 25C in 50 mM Tris-HCl buffer (pH 7.0)
7.55
-
canavanine
-
-
0.31
-
D-Arginine
-
-
6.02
-
Homoarginine
-
-
6
-
L-canavanine
-
pH 7.3, 30C
7
-
L-Homoarginine
-
pH 7.3, 30C
8
-
nitrate
-
with L-arginine as substrate
-
0.008
-
rutin
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.015
-
Ag+
-
at 25C in 50 mM Tris-HCl buffer (pH 7.0)
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00227
-
-
formation of arginine phosphate, enzyme from crude extract
0.00312
-
-
formation of ATP, enzyme from crude extract
0.245
-
-
homogenous muscle enzyme
0.2539
-
-
cell extract
0.288
-
-
cell extract
8.78
-
-, Q004B5
at pH 8.6 and 30C
40.3
-
A7YVI5, -
-
53.78
-
-
mutant enzyme R330K, pH and temperature not specified in the publication
248
-
-
-
268.6
-
-
recombinant wild type enzyme, pH and temperature not specified in the publication
390.5
-
-
after purification
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
-
-
synthesis of ATP
6
-
-
synthesis of arginine and ATP
6
-
Isostychopus badonotus
-
optimal pH for the formation of arginine and ATP
6.1
-
-
synthesis of ATP
6.2
6.3
-
synthesis of ATP
6.3
-
-
synthesis of ATP, 20 mM phosphate buffer
6.5
7.5
-
reverse reaction
6.6
-
-
optimal pH for the formation of arginine and ATP
6.6
-
-
formation of arginine and ATP
6.9
-
-
synthesis of ATP, 20 mM Tris-HCl buffer
7.1
7.2
-
synthesis of ATP
7.2
-
-
formation of ATP, enzyme from third stage juveniles
7.3
-
-
formation of ATP, enzyme from adult
7.8
-
-
formation of arginine phosphate, enzyme from third-stage juveniles
7.9
8.5
-
formation of arginine phosphate, enzyme from adult
8
-
Isostychopus badonotus, Strongylocentrotus purpuratus
-
optimal pH for the formation of arginine phosphate and ADP
8
-
-
formation of arginine phosphate and ADP
8.2
-
-
synthesis of N-phospho-L-arginine, 20 mM Tris-HCl buffer or 20 mM phosphate buffer
8.3
-
-
synthesis of N-phospho-L-arginine
8.5
-
-
synthesis of arginine phosphate and ADP
8.5
-
-
forward reaction
8.5
-
B1PVZ9
in the process of forward reaction
8.6
-
-
synthesis direction of phosphoarginine and ADP
8.7
8.8
-
synthesis of N-phospho-L-arginine
9
-
-
synthesis of N-phospho-L-arginine
9.2
-
-
synthesis of N-phospho-L-arginine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.2
-
pH 5.0: about 30% of maximal activity, pH 8.2: about 30% of maximal activity, ATP synthesis
5.5
7.5
-
pH 5.5: about 90% of maximal activity, pH 7.5: about 60% of maximal activity, synthesis of ATP
5.5
8
-
pH 5.5: about 90% of maximal activity, pH 8.0: about 70% of maximal activity, no activity at pH 5.0, synthesis of ATP
5.6
7.5
-
about 15% of maximal activity, pH 5.6: about 85% of maximal activity, pH 7.5: about 80% of maximal activity, synthesis of arginine and ATP; pH 5.3
5.9
6.8
-
pH 5.9: about 35% of maximal activity, pH 6.8: about 55% of maximal activity, synthesis of ATP, 20 mM phosphate buffer
6.3
9
-
pH 6.3: about 65% of maximal activity, pH 9.0: about 70% of maximal activity, synthesis of N-phospho-L-Arg
6.5
7.3
-
pH 6.5: about 45% of maximal activity, pH 9.0: about 45% of maximal activity, synthesis of ATP, 20 mM Tris-HCl buffer
7
10
-
pH 7.0, about 30% of maximal activity, pH 10.0: about 35% of maximal activity, synthesis of N-phospho-L-arginine
7
10.5
-
pH 7.0: about 40% of maximal activity, pH 10.5: about 35% of maximal activity, synthesis direction of phosphoarginine and ADP
7.2
9
-
pH 7.2: about 45% of maximal activity, pH 9.0: about 55% of maximal activity, synthesis of arginine phosphate and ADP
7.5
10
E2JE77, -
-
7.5
9
-
about 50% of maximal activity at pH 7.5 and pH 9.0, synthesis of N-phospho-L-arginine, 20 mM Tris-HCl buffer
8
10.5
-
pH 8.0: about 60% of maximal activity, pH 10.0: about 70% of maximal activity, synthesis of N-phospho-L-Arg
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
synthesis direction of phosphoarginine and ADP
30
-
B1PVZ9
in the process of forward reaction
45
-
-
synthesis of ATP and synthesis of N-phospho-L-Arg
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
60
-
10C: about 50% of maximal activity, 60C: about 60% of maximal activity
10
60
-
10C: about 40% of maximal activity, 60C: about 40% of maximal activity
10
70
-
10C: about 55% of maximal activity, 70C: about 40% of maximal activity, synthesis direction of phosphoarginine and ADP
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
Q4AED1, Q4AED2, -
calculated from sequence
5.82
-
-
theoretical value calculated from amino acid sequence
6.1
-
E2JE77, -
calculated from amino acid sequence
6.21
-
Q4AED1, Q4AED2, -
calculated from sequence of cDNA
6.3
-
-
2D-SDS-PAGE
6.3
-
-
recombinant enzyme, isoelectric focusing
6.5
-
-
isoelectric focusing
6.5
-
-
native enzyme, isoelectric focusing
6.7
-
-, Q4AEC4
calculated from sequence
7
-
-
theoretical value calculated from amino acid sequence
7.1
-
-, D5FLG2
calculated from amino acid sequence
7.2
-
Q4AED1, Q4AED2, -
calculated from sequence
8.28
-
A7YVI5, -
calculated from sequence
8.38
-
A7YVI5, -
calculated from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
activity increases continuously during the exponential phase of growth
Manually annotated by BRENDA team
B0FRF9
very low mRNA expression
Manually annotated by BRENDA team
E2JE77, -
lowest expression
Manually annotated by BRENDA team
B0FRF9
very low mRNA expression
Manually annotated by BRENDA team
-
male and female
Manually annotated by BRENDA team
B0FRF9
very low mRNA expression
Manually annotated by BRENDA team
B0FRF9
very low mRNA expression
Manually annotated by BRENDA team
-
third-stage juvenile
Manually annotated by BRENDA team
E2JE77, -
walking leg
Manually annotated by BRENDA team
Isostychopus badonotus
-
-
Manually annotated by BRENDA team
-
arginine kinase up-regulation under hypoxia may indicate a provision for oxygen re-supply after anaerobiosis
Manually annotated by BRENDA team
B0FRF9
highest mRNA expression in the muscle
Manually annotated by BRENDA team
E2JE77, -
highest expression
Manually annotated by BRENDA team
B0FRF9
subcuticular skin, lowest mRNA expression in the skin
Manually annotated by BRENDA team
Pleocyemata sp.
-
-
Manually annotated by BRENDA team
H9BZ68
the enzyme is more abundant in the thorax, where it represents up to 2% of the total soluble protein, compared to head or abdomen
Manually annotated by BRENDA team
additional information
-
no activity in sperm
Manually annotated by BRENDA team
additional information
Q2F5T5
not detected in hemocytes
Manually annotated by BRENDA team
additional information
-
not detected in the cuticle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q2F5T5
main localization
Manually annotated by BRENDA team
A7YVI5, -
presence of a signal targeting peptide presumably targeting this protein to cytosol or endoplasmic reticulum
Manually annotated by BRENDA team
A7YVI5, -
presence of a signal targeting peptide presumably targeting this protein to cytosol or endoplasmic reticulum
Manually annotated by BRENDA team
-
no microcompartmentation
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
36000
-
-
gel filtration
37400
-
-
-
40000
-
-
sedimentation equilibrium centrifugation
40000
-
-
gel filtration
40000
-
-
equilibrium sedimentation
40000
-
-
gel filtration
40000
-
Isostychopus badonotus, Strongylocentrotus purpuratus
-
SDS-PAGE
40000
-
A4F2K7, -
SDS-PAGE
40000
-
-, Q004B5
SDS-PAGE
40000
-
B0FRF9
SDS-PAGE
40570
-
-
SDS-PAGE
41500
-
-
isoform AK1, estimated from SDS-PAGE
42000
-
-
sedimentation equilibrium centrifugation
42000
-
-
-
42000
-
Q2F5T5
SDS-PAGE
42890
-
Q4AED1, Q4AED2, -
calculated from sequence of cDNA
43000
-
-
gel filtration
43400
-
-
isoform AK2, estimated from SDS-PAGE
45380
-
A7YVI5, -
calculated from sequence of cDNA
55000
-
-
gel filtration
80000
-
-
gel filtration
80000
-
-
SDS-PAGE
80000
-
Q4AED1, Q4AED2, -
fusion proteins with hexameric His tag, gel filtration; fusion proteins with hexameric His tag, gel filtration
81000
-
-
gel filtration
82000
-
-, Q4AEC4
calculated from sequence
150000
-
-
sedimentation equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE; x * 40500, SDS-PAGE
?
-
x * 37687, calculation from amino acid sequence determined from cyanogen bromide fragments
?
-
x * 40100, calculation from nucleotide sequence
?
-
x * 40238, calculation from nucleotide sequence
?
-
x * 80000, SDS-PAGE
?
-, Q9NKV6
x * 40500, SDS-PAGE
?
-, Q9NKV5
x * 40500, SDS-PAGE
?
Q9NKV4, -
x * 40500, SDS-PAGE
?
-
x * 40201, calculation from nucleotide sequence
?
A7YVI5, -
x * 45376, calculated from sequence
?
-
x * 40000, SDS-PAGE
?
E2JE77, -
x * 40000, calculated from amino acid sequence
?
-
x * 40000, calculated from amino acid sequence
?
-
x * 38000, SDS-PAGE
?
-, D5FLG2
x * 45341, recombinant enzyme, calculated from amino acid sequence; x * 85000, recombinant enzyme fused to maltose-binding protein, SDS-PAGE
?
-
x * 40000, native and recombinant enzyme, SDS-PAGE
?
-
x * 80000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
-
x * 85000, maltose-binding protein-fused enzyme, SDS-PAGE
?
H9BZ68
x * 40000, SDS-PAGE
?
Phytomonas sp. Jma
-
x * 40000, SDS-PAGE
-
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 40000
dimer
-
2 * 42000, SDS-PAGE
dimer
Q4AED1, Q4AED2, -
2 * 40000, Superdex 75 gel filtration; 2 * 42273, calculated from sequence; 2 * 42887, calculated from sequence
homodimer
-
2 * 40000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 42000
monomer
-
1 * 37400
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 79933, calculation from nucleotide sequence; 1 * 80000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
tetramer
-
4 * 38000-39000, sedimentation equilibrium in presence of 6 M guanidine hydrochloride, gel filtration in 8 M urea
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structures of mutant enzymes E314D at 1.9 A and E225Q at 2.8 A resolution shows that the precise alignment of substrates is subtly distorted
-
in complex with L-ornithine, L-citrulline, imino-L-ornithine, and D-arginine, hanging drop vapor diffusion method, using 26% (w/v) PEG 6000, 50 mM HEPES, and 100 mM MgCl2 at a pH of 8.0
-
polyethylene glycol precipitation of recombinant enzyme. Crystallization as a transition state analog
-
hanging drop vapour diffusion method, the crystallographic structure of the alanine mutant at 2.3 A resolution, determined as a transition state analogue complex with arginine, nitrate, and MgADP2-, is nearly identical to wild type structure
Pleocyemata sp.
-
hanging drop method, structure of ligand-free TcAK is determined by molecular replacement methods and refined at 1.9 A resolution; hanging drop vapour diffusion method using 2.5 M ammonium sulfate, and 0.1 M Tris-HCl, pH 7.5
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.1
-
-
25C, 15 min, 70% loss of activity
5.4
-
-
25C, 15 min, 20% loss of activity
6
9.1
-
25C, 15 min, stable
8.5
-
-
30C, 3 h, stable
9
10
-
the enzyme displays no obvious change when the pH value is below 9.0, but the original band of the enzyme is faint and the degraded fragments of the enzyme are observed when it is incubated at pH 9.5 and 10.0 for 1 h
10
11
-
at pH 10.0, the relative activity is slightly reduced, in the pH range of 1010.5, the relative activity decreases by almost 60% and above pH 11.0 the enzyme fully loses activity
11
13
-
pH 11.0 is required to cause the complete loss of AK activity of the alkaline unfolded enzyme, the high pH denatured enzyme has some residual secondary and tertiary structure even at pH 13
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
10 min, inactivation above
30
40
-
the enzyme is relatively stable below 30C, but the original bands become faint and the bands of aggregated enzyme (above 70 kDa) appear when the temperature is above 40C
30
-
-
pH 8.5, 3 h, stable
30
-
-
10 min, wild-type enzyme, and mutant enzymes P272D, P272G and P272R are stable
35
-
-
10 min, stable
40
-
-
10 min, 100 mM Tris-HCl buffer, pH 8.0, 15% loss of activity. 10 min, 100 mM Tris-HCl buffer, pH 7.0, 16% loss of activity
40
-
-
10 min, 100 mM Tris-HCl buffer, pH 8.0, 34% loss of activity. 10 min, 100 mM Tris-HCl buffer, pH 7.0, 46% loss of activity
40
-
-
10 min, 21% loss of activity
40
-
-
10 min, wild-type enzyme loses about 10% of its activity, mutant enzyme P272D loses about 30% of its activity, mutant enzyme P272G loses about 25% of its activity and mutant enzyme P272R loses about 35% of its activity
45
65
-
the wild type enzyme can retain its activity well at temperatures lower than 48C, and then its activity shows a steep decrease from 45 to 60C and completely loses its activity at temperatures above 65C. The melting temperature is at about 56C
45
65
-
the wild type enzyme retains its activity well at temperatures lower than 48C, and then its activity shows a steep decrease from 45 to 60C and completely loses its activity at temperatures above 65C
45
-
-
inactivation
45
-
-
10 min, stable up to
46
60
-
the activity of wild type enzyme changes a little after heat treatment for 10 min at temperatures below 45C. A steep decrease of activity is observed after 10 min between 45 and 60C, and a complete loss of activity occurs above 65C. The midpoint of thermal inactivation of wild type enzyme is at about 52C
50
-
-
10 min, 50% loss of activity
50
-
-
10 min, wild-type enzyme loses about 40% of its activity, mutant enzyme P272D loses about 90% of its activity, mutant enzyme P272G loses about 85% of its activity and mutant enzyme P272R loses about 90% of its activity
55
-
-
10 min, complete loss of activity
additional information
-
-
unstable to heat
additional information
-
-
unstable to heat
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the N-terminal of arginine kinase plays an important role in maintaining the conformational stability and catalytic function of the enzyme
-
the substrate-bound structure of the two-domain enzyme is stabilized by the bond between H60 and D197
-
reversible inactivation by treatment with 8 M urea, reactivation is promoted by thiols and inhibited by divalent metal ions
-
stable to repeated freezing/thawing
-
the unfolding transition curves of mutations P272R and P272G are almost identical to wild-type enzyme for all conditions at GdnHCl concentrations varying from 0.1 to 6 M
-
more stable in 100 mM Tris-HCl buffer at pH 8.0 than in 100 mM phosphate buffer at pH 7.0
-
the substrate-bound structure of the two-domain enzyme is stabilized by the bond between H60 and D197
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DMSO
-
prevents arginine kinase unfolding and inactivation that is due to a guanidine hydrochloride denaturant by reducing the inactivation rate constants, increasing the transition free energy changes and increasing the value for the midpoint of denaturation
Glycerol
-
prevents arginine kinase unfolding and inactivation that is due to a guanidine hydrochloride denaturant by reducing the inactivation rate constants, increasing the transition free energy changes and increasing the value for the midpoint of denaturation
guanidine-HCl
-
2.0 M guanidine hydrochloride results in almost complete unfolding of arginine kinase. When adding the osmolytes (Pro, sucrose, DMSO, glycerol) to the unfolding system, 2.0 M guanidine hydrochloride only brings about a partial red shift compared to the samples without osmolyte. Osmolytes stabilize the arginine kinase conformation against guanidine hydrochloride in a concentration-dependent manner
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C or -10C, at least 3 months
-
4C, slow loss of activity during prolonged storage, can partially be reactivated by addition of 0.1% w/v 2-mercaptoethanol
-
-20C, 10 mM Tris-HCl buffer, pH 8.5, activity gradually decreases, but can be restored by addition of 1 mM 2-mercaptoethanol
-
4C, 3 months, 68% loss of activity
-
0C, purified enzyme on ice, 24 h, 75% loss of activity
-, Q1DA50
-80C, several months
-
-20C, 10 mM Tris-HCl buffer, pH 8.5, activity gradually decreases, but can be restored by addition of 1 mM 2-mercaptoethanol
-
refrigerated, 80% saturated ammonium sulfate, 20 mM L-Arg, 100 mM 2-mercaptoethanol, pH 7.0. 50% loss of activity in 8-10 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Ni-NTA column chromatography
-
Ni2+-nitrilotriacetic acid column chromatography and Superdex 200HR 10/30 gel filtration
-
Ni2+-NTA column chromatography and Superdex 200HR 10/30 gel filtration
-
recombinant enzyme
-
amylose resin column chromatography
-, D5FLG2
Ni-NTA column chromatography, gel filtration
Q2F5T5
Ni2+-NTA column chromatography
Q2F5T5
amylose resin column chromatography
-
Ni2+-NTA agarose column chromatography
-
DEAE-Sepharose column chromatography
-
-
Isostychopus badonotus
-
recombinant enzyme from Escherichia coli
-
three-dimensional crystal structure of an arginine kinase transition-state analogue complex refined at 1.2 A resolution
-
glutathione Sepharose 4B column chromatography
B0FRF9
; Sephacryl S-200HR gel filtration and DEAE Sepharose CL-6B fast flow chromatography
-
Sephacryl S-200 HR gel filtration and DEAE Sepharose CL-6B fast flow column chromatography
-
Sephadex G-75 gel filtration
-
Ni2+-NTA agarose column chromatography
H9BZ68
the crude AK-1 fusion protein fused with maltose binding protein is purified using pMAL protein fusion and purification system protocol
E2JE77, -
CM-cellulose column chromatography, Sephacryl S-100 gel filtration, and DEAE-Sepharose column chromatography
B1PVZ9
nickel affinity column chromatography
-
MBPTrap HP column chromatography
-, Q1DA50
enzyme form AK1 and enzyme form AK2
-
-
Pleocyemata sp.
-
recombinant enzyme
-
Amberlite IR120BNA column chromatography and reverse-phase high performance liquid chromatography
Q4AED1, Q4AED2, -
ammonium sulfate precipitation and Q Sepharose column chromatography
-
amylose resin column chromatography
A7YVI5, -
recombinant fusion protein
-
Ni-column chromatography and Superdex-75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNAs of the two-domain arginine kinase and its separated domains 1 and 2 from Anthopleura japonicus, are cloned into the plasmid pMAL, and recombinant enzymes are expressed in Escherichia coli as MBP fusion proteins
O15992
expressed in Escherichia coli BL21 cells
-
amplification of cDNA for arginine kinase
A6XH11, -
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
expressed in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli BL21
-
gene cloned and inserted into the prokaryotic expression plasmid pET-21b, expression in a soluble and functional form in Escherichia coli
-
expressed as a fusion protein with maltose-binding protein in Escherichia coli TB1 cells
-, D5FLG2
expressed as a His-tagged fusion protein in Escherichia coli BL21 cells
Q2F5T5
expressed as fusion proteins with the maltose-binding protein in Escherichia coli. When expressed alone, domain 1 displays minimal activity. When expressed alone, domain 2 has significantly higher activity and catalytic efficiency that the two-domain wild-type AK, when domain 1 is inactivated using the Y68A mutation, activity is about 50% of the wild-type enzyme and when domain 2 is inactivated using the Y68A mutation, activity is retained at about 12% of the wild-type level
-, Q4AEC4
expressed as maltose-binding protein enzyme fusion protein in Escherichia coli TB-1 cells
-
expressed in Escherichia coli as a fusion with maltose-binding protein; expression of Cissites arginine kinase protein in Escherichia coli as a fusion with maltose-binding protein
A4F2K7, -
amplification of cDNA for arginine kinase
B0L6Z8, -
domain 2 is separated from the two-domain enzyme and expressed in Escherichia coli, domain 2 still exhibits activity. Expression of mutants of domain 2 in Escherichia coli: H60G, H60R and D197G
-
expression in Escherichia coli
-
expressed in Escherichia coli Rosetta cells
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) codon plus cells by prokaryotic expression plasmid pGEX-4T-2 as glutathione S-transferase arginine kinase fusion protein
B0FRF9
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
expressed in Escherichia coli by two prokaryotic expression plasmids, pET-30a and pET-28a28a. The recombinant protein is expressed as inclusion bodies using pET-30a. Using expression plasmid, pET-28a, and changing the expression conditions results in a soluble and functional form of arginine kinase
-
expression of wild-type and mutant enzymes (Y75F, Y75D, P272G, P272R, Y75F/P272G and Y75D/P272R) in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli M15 cells
H9BZ68
expressed in Escherichia coli BL21(DE3) cells
E2JE77, -
the His6-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
-
cloned in prokaryotic expression plasmid pET-28a, and then expressed in Escherichia coil strain Rosetta in dissoluble form
B1PVZ9
expressed in Escherichia coli Rosetta cells
-
amplification of cDNA for arginine kinase
A6XH14, -
amplification of cDNA for arginine kinase. There are three unique arginine kinase genes in the choanoflagellate Monosiga brevicollis
B0L6Z7, -
amplification of cDNA for arginine kinase
B0L6Z9, -
expressed in Escherichia coli BL21(DE3) cells
-, Q1DA50
expression in Escherichia coli
Pleocyemata sp.
-
expression in Escherichia coli as a histidine-tagged protein
-
cloning of cDNAs into pMAL plasmid and expression in Escherichia coli as a fusion protein with MBP tag or hexameric His tag; cloning of cDNAs into pMAL plasmid and expression in Escherichia coli as a fusion protein with MBP tag or hexameric His tag; expressed in Escherichia coli
Q4AED1, Q4AED2, -
isoform AK2 fused to maltose-binding protein is expressed in Escherichia coli TB1 cells
-
expressed in Escherichia coli BL21 cells
-
amplification of cDNA for arginine kinase
A6XH17, -
cloned it in pMAL plasmid and expressed it in Escherichia coli as a fusion protein with maltose-binding protein; expressed in Escherichia coli as a fusion protein with maltose-binding protein
A7YVI5, -
expressed as a fusion protein with maltose-binding protein in Escherichia coli JM109 cells
-
open reading frame of Toxocara canis arginine kinase is cloned into the BamHI/SalI site of pMAL-c2X. The maltose-binding protein (MBP)-Toxocara canis arginine kinase fusion protein is expressed in Escherichia coli TB1 cells by induction with 1 mM IPTG at 25C for 24 h
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme activity gradually increases during embryonic development
-
the expression level of the enzyme increases more than 10fold 24 h post inoculation of nucleopolyhedrovirus in Bombyx mori strains NB and BC8
Q2F5T5
the levels of AK-1 mRNA transcripts sharply increase until 12 h post-injection with IHHNV
E2JE77, -
the enzyme activity gradually increases during embryonic development
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D62E
O15992
introduction of Glu at position 62 in isolated domain 2. The catalytic efficiency of D2/D62E is similar to that of the two-domain wild-type enzyme. This replacement does not alter synergistic substrate binding relative to wild-type domain 2
Y68G
-
the mutation in domain 1 or 2 leads to almost no catalytic activity
D57A
-
the mutation causes pronounced loss of activity and substrate synergism, and distinct conformational changes
D57E
-
most of the kinetic parameters are similar to those of wild type enzyme. A small decrease in Kd/Km and kcat/Km (L-Arg) values indicate a slight loss of substrate synergism and catalytic efficiency
D62G
-
2.3fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 3.5% of the wild-type value
D62_F63delinsDGF
-
2.9fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 0.01% of the wild-type value
delN56_V58
-
inactive mutant enzyme
E314D
-
significantly decreased activity
E314Q
-
significantly decreased activity
E314V
-
turnover number is 0.000019% of the wild-type value
E314V
-
significantly decreased activity
F315A
-
modest AK activity
F315H
-
modest AK activity
F315Y
-
modest AK activity
F63G
-
20.48fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 12.9% of the wild-type value
H64G
-
1.53fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 70.4% of the wild-type value
Q53A
-
the mutation causes pronounced loss of activity and substrate synergism, and distinct conformational changes
Q53A/D57A
-
the changes in kinetic parameters as well as the loss of substrate synergism of the double mutant are more severe than that of Q53A and D57A single mutant enzymes. In addition, the double mutant has the lowest affinity for ATP
Q53E
-
most of the kinetic parameters are similar to those of wild type enzyme. A small decrease in Kd/Km and kcat/Km (L-Arg) values indicate a slight loss of substrate synergism and catalytic efficiency
R193G
-
3.5fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 1.7% of the wild-type value
S282G
-
2.81fold increase in KM-value for L-arginine compared to wild-type value, 16.34fold increase in KM-value for ATP compared to wild-type value, turnover number is 88.7% of the wild-type value
S312G/E314V/F315D/E317A/S318A/G321S
-
slight arginine kinase activity
S312R/F315H/V319E
-
modest AK activity
W208A
-
mutant enzyme shows 70.3% of the wild-type enzyme in the forward reaction. Mutation makes the enzyme susceptible to heat and denaturants, sich as guanidine HCl
W218A
-
mutation causes almost complete loss of activity and decreases the melting temperature in differential scanning calometry profiles and decreases stability against guanidine hydrochloride denaturation
Y89R
-
1.35fold increase in KM-value for L-arginine compared to wild-type value, turnover number is 35.9% of the wild-type value
A105S
-, D5FLG2
the mutant shows decreased Km values and turnover number for L-Arg (about 120% affinity) and ATP as well as slightly decreased catalytic efficiency (to about 90%) compared to the wild type enzyme
A105S/S106G
-, D5FLG2
the mutant shows increased Km values and turnover number for L-Arg (about 70% affinity) and ATP as well as decreased catalytic efficiency (to about 70%) compared to the wild type enzyme
S106G
-, D5FLG2
the mutant shows increased Km values and turnover number for L-Arg (about 60% affinity) and ATP as well as decreased catalytic efficiency (to about 60%) compared to the wild type enzyme
Y68A
-, Q4AEC4
introduction of a Y68A mutation in both domains virtually abolishes catalytic activity. Significant residual activity is observed, when the Y68A mutation is introduced only into domain 2 of the two-domain enzyme. A similar mutation in domain 1 of the two domain enzyme reduces activity to a much lower extent
D197G
-
mutant of domain 2, affinity for Arg in mutant enzyme is reduced considerably, accompanied by a decrease in Vmax
H60G
-
mutant of domain 2, affinity for Arg in mutant enzyme is reduced considerably, accompanied by a decrease in Vmax
H60R
-
mutant of domain 2, affinity for Arg in mutant enzyme is reduced considerably, accompanied by a decrease in Vmax
K193G
Crassostrea sp.
-
turnover number is 68% of the wild-type value, KM-value for L-arginine is 4.1fold higher than wild-type value, Km-value for ATP is 2.2fold higher than wild-type value
K194R
Crassostrea sp.
-
turnover number is 85% of the wild-type value, KM-value for L-arginine is 4.5fold higher than wild-type value, Km-value for ATP is 1.3fold higher than wild-type value
N62D
Crassostrea sp.
-
turnover number is 88% of the wild-type value, KM-value for L-arginine is 1.1fold lower than wild-type value, Km-value for ATP is 1.2fold higher than wild-type value
N62D/K193R
Crassostrea sp.
-
turnover number is 89% of the wild-type value, KM-value for L-arginine is 2.3fold higher than wild-type value, Km-value for ATP is 1.6fold higher than wild-type value
N62G
Crassostrea sp.
-
turnover number is 53% of the wild-type value, KM-value for L-arginine is identical to wild-type value, Km-value for ATP is 1.2fold lower than wild-type value
N62G/K193G
Crassostrea sp.
-
turnover number is 51% of the wild-type value, KM-value for L-arginine is 4.1fold higher than wild-type value, Km-value for ATP is 3.9fold higher than wild-type value
E225A
-
turnover number is 0.03% of the wild-type value
E225D
-
KM-value for ADP is 2.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.14fold higher than wild-type value, turnover number is 0.24% of the wild-type value
E225Q
-
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.4fold higher than wild-type value, turnover number is 0.3% of the wild-type value
E225Q/E314Q
-
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 2.3fold higher than wild-type value, turnover number is 0.2% of the wild-type value
E314D
-
KM-value for ADP is 1.3fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.56fold higher than wild-type value, turnover number is 1.7% of the wild-type value
R312G/E314V/H315D/E317A/E319V
-
KM-value for ADP is 1.5fold lower than the wild-type value, KM-value for N-phospho-L-arginine is 1.5fold higher than wild-type value, turnover number is 83% of the wild-type value
R330K
-
the mutant enzyme is more susceptible to oxidation than the wild type enzyme and shows 20% of wild type activity
I121D
-
the mutation leads to pronounced loss of activity and structural stability. The mutation also leads to serious aggregation during heat-and guanidine hydrochloride-induced denaturation and refolding from the guanidine hydrochloride-denatured state
I121G
-
the mutation leads to pronounced loss of activity and structural stability. The mutation also leads to serious aggregation during heat-and guanidine hydrochloride-induced denaturation and refolding from the guanidine hydrochloride-denatured state
I121K
-
the mutation leads to pronounced loss of activity and structural stability. The mutation also leads to serious aggregation during heat-and guanidine hydrochloride-induced denaturation and refolding from the guanidine hydrochloride-denatured state
I121L
-
the almost has no effect on AK activity and structural stability
L113D
-
the mutant shows strongly decreased activity compared to the wild type enzyme
L113G
-
the mutant shows decreased activity compared to the wild type enzyme
L113I
-
the mutant shows about wild type Km and kcat values
L113K
-
the mutant shows strongly decreased activity (10.3% catalytic efficiency) compared to the wild type enzyme
P272D
-
activity of the mutant P272D is about 40% of that of wild-type enzyme. The binding affinity of arginine and ATP in the P272D is much smaller than that of wild-type enzyme, as indicated by an about 2- to 3fold increase of the Km values for ATP and arginine. The mutation impairs the tertiary structures of the enzyme. Decrease in thermal stability
P272G
-
the synergism is almost completely lost. Fluorescence spectrum shows a red shift
P272G
-
decrease in thermal stability
P272R
-
the synergism is almost completely lost. Fluorescence spectrum shows a red shift
P272R
-
decrease in thermal stability
Y75D
-
mutant shows strong synergism. Fluorescence spectrum shows a red shift
Y75D/P272R
-
characteristics similar to those of the wild-type enzyme
Y75F
-
mutant shows strong synergism. Fluorescence spectrum shows a red shift
Y75F/P272G
-
the synergism is almost completely lost. Fluorescence spectrum shows a red shift
D62E
-
the mutant retains almost 90% of the wild type activity
D62G
-
the mutant has a pronounced loss in activity
R193G
-
the mutant has a pronounced loss in activity
R193K
-
the mutant retains almost 90% of the wild type activity
D62E
-, Q9NKV6
3.3% of Vmax of recombinant wild-type enzyme, Km-value for L-Arg is 99% of that of the wild-type enzyme
D62G
-, Q9NKV6
0.6% of Vmax of recombinant wild-type enzyme
R193G
-, Q9NKV6
,1.5% of Vmax of recombinant wild-type enzyme
S63G
-, Q9NKV6
5.1% of Vmax of recombinant wild-type enzyme, Km-value for L-Arg is 516% of that of the wild-type enzyme
S63T
-, Q9NKV6
0.3% of Vmax of recombinant wild-type enzyme
Y68S
-, Q9NKV6
mutant enzyme without activity
C271A
Pleocyemata sp.
-
1300fold decrease in turnover number, in presence of 1 mM Cl-. 3.6fold increase in Km-value for N-phospho-L-arginine, 7.5fold increase in Km-value for ATP, in presence of 1 mM Cl-
C271D
Pleocyemata sp.
-
86.7fold decrease in turnover number, in presence of 1 mM Cl-. 9.8fold increase in Km-value for N-phospho-L-arginine, 2.5fold increase in Km-value for ATP, in presence of 1 mM Cl-
C271N
Pleocyemata sp.
-
4727fold decrease in turnover number, in presence of 1 mM Cl-. 2.7fold increase in Km-value for N-phospho-L-arginine, 4.3fold increase in Km-value for ATP, in presence of 1 mM Cl-
C271S
Pleocyemata sp.
-
1486fold decrease in turnover number in presence of 1 mM Cl-. 16.8fold increase in Km-value for N-phospho-L-arginine, 5fold increase in Km-value for ATP in presence of 1 mM Cl-
G54A
-
the mutant shows considerably increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme
G54I
-
the mutant displays undetectable enzymatic activity
G54L
-
the mutant displays undetectable enzymatic activity
G54S
-
the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme
G54V
-
the mutant displays undetectable enzymatic activity
L64A
-
the mutant displays undetectable enzymatic activity
L64G
-
the mutant displays undetectable enzymatic activity
L64I
-
in the mutant, the affinity for L-arginine is greatly increased (9.5fold that of the wild type), whereas its affinity for D-arginine is increased 2.9fold
L64V
-
the mutant shows a 1.7fold decrease in affinity for L-arginine, but unchanged affinity for D-arginine
N320A
-
the mutant shows considerably reduced enzymatic activity (17.1% for L-arginine and 5.19% for D-arginine compared to the wild type enzyme)
N320D
-
the mutant shows considerably reduced enzymatic activity (32.4% for L-arginine and 48.4% for D-arginine compared to the wild type enzyme)
N320E
-
the mutant shows considerably reduced enzymatic activity (52.3% for L-arginine and 10.1% for D-arginine compared to the wild type enzyme)
N320H
-
the mutant shows considerably reduced enzymatic activity (29.5% for L-arginine and 10.2% for D-arginine compared to the wild type enzyme)
N320K
-
the mutant shows considerably reduced enzymatic activity (0.612% for L-arginine and 0.489% for D-arginine compared to the wild type enzyme)
N320Q
-
the mutant shows considerably reduced enzymatic activity (8.97% for L-arginine and 2,6% for D-arginine compared to the wild type enzyme)
N320R
-
the mutant shows considerably reduced enzymatic activity (4.11% for L-arginine and 1.46% for D-arginine compared to the wild type enzyme)
Y89Q
-
the mutant shows increased catalytic efficiency for L-arginine and D-arginine compared to the wild type enzyme
D62G
O15992
introduction of Gly at position 62 in isolated domain 2. The catalytic efficiency of the D2/D62G mutant is decreased to 13% that of wild-type domain 2
additional information
-
the kcat value of the mutant with six Lys residues in the linker region between domains D1 and D2 is reduced to 27.6% that of the two-domain wild-type enzyme
L65G
-
turnover number is 0.0011% of the wild-type value
additional information
-
deletion mutants of arginine kinase are constructed. The first 4, 6, 8 and 10 amino acids of the N-terminal are deleted. The deletion mutants assume less compact conformations compared to the wild-type, whereas no significant changes of the secondary or the quaternary structures are observed, implying that the deletions cause a perturbation in the tertiary structure or the hydrodynamic properties of the enzyme. The enzymatic and denaturing measurements show that removal of the N-terminal residues decrease the activity and stability of the enzyme markedly. The instability increases in accord with the increased number of amino acid residues removed from the N-terminal of the enzyme
E314Q
-
KM-value for ADP is 1.2fold higher than the wild-type value, KM-value for N-phospho-L-arginine is 1.1fold higher than wild-type value, turnover number is 0.3% of the wild-type value
additional information
-
double mutant Val268insertion/Phe270deletion: enzyme with significaltly decreased specific activity compared with both the native and the recombinant wild-type enzyme, no detectable change in guanidine substrate specificity
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
there are at least two intermediates in the refolding of urea-denatured dimeric arginine kinase. I1 (existing in 1.8-1.4 M urea) and I2 (existing in 0.8-0.4 M urea). I1 is a monomeric globular intermediate. I2 is an active native-like intermediate. The refolding of arginine kinase possesses a burst phase, fast phase and slow phase, which involves at least the burst phase intermediates
-
the folding rate partly recovers to 60% as the inducing concentration of 1,1,1,3,3,3-hexafluoroisopropanol increases to 10% (v/v)
Q4KY22
addition of 1% (v/v) Tween-20 and 0.6% (w/v) SDS to the dilution system leads to higher renaturation efficiency
-
after denaturation, the recombinant AK is successfully renatured and confirmed to be enzymatically active. Addition of Tween-20 and SDS to the dilution system lead to higher renaturation efficiency
-
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
B3TNF9
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF8
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF7
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF6
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF5
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF4
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF3
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNG1
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF1, Q9U9J4
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura; evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNC8
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
Q9NH48
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF0
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE9
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE8
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE7
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE6
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE5
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE4
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE3
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE2
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNF2
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE1
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TND9
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNE0
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
Q9NH47
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNG0
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TND7
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TND8
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
Q9GYX1
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TND6
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
drug development
-
the enzyme could be a useful chemotherapeutic target for the control of cockroach proliferation
analysis
B3TND5
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
medicine
-
the recombinant enzyme may be used to identify a group of polysensitized indoor allergic patients and for immunotheraphy of theses individuals
analysis
Portunus sp.
B3TND4
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
-
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
-
analysis
B3TND3
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TND2
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TND1
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
diagnostics
-
development of IgG-ELISA based on antiserum prepared against the recombinant arginine kinase of Toxocara canis. The recombinant-arginine kinase based IgG-ELISA could be applied for immunodiagnosis of human toxocariasis
medicine
A7YVI5, -
this enzyme as a possible novel chemotherapy target for VLM syndrome in humans
medicine
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the enzyme is a possible target for chemotherapy
medicine
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arginine kinase is a possible chemotherapy target for Chagas disease
analysis
B3TND0
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura
analysis
B3TNC9
evaluation of a region of the nuclear gene that encodes arginine kinase for phylogenetic analysis of the Brachyura