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Information on EC 2.7.3.3 - arginine kinase and Organism(s) Penaeus vannamei and UniProt Accession Q004B5

for references in articles please use BRENDA:EC2.7.3.3
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Penaeus vannamei
UNIPROT: Q004B5 not found.
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The taxonomic range for the selected organisms is: Penaeus vannamei
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
arginine kinase, argk, arginine phosphokinase, pyak3, tcak1, mnak2, tcak2, pyak2, pyak4, tbak3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine 5'-triphosphate-arginine phosphotransferase
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-
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adenosine 5'-triphosphate: L-arginine phosphotransferase
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AK
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arginine phosphokinase
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ATP: arginine N-phosphotransferase
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ATP:L-arginine N-phosphotransferase
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kinase, arginine (phosphorylating)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ATP:L-arginine Nomega-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-70-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-Arg
ADP + omega-N-phospho-L-Arg
show the reaction diagram
arginine kinase is an allergenic protein
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-
?
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
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-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-arginine
ADP + Nomega-phospho-L-arginine
show the reaction diagram
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-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
the enzyme activity is inhibited by 10 mM 2-oxoglutarate
ATP
the enzyme is inhibited by 200 mM ATP
D-glucose
the enzyme is inhibited by 50 mM D-glucose, almost all arginine kinase activity is lost after treatment with 200 mM D-glucose
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
after treatment with 10 mM ATP, the enzyme activity significantly increases
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.78
at pH 8.6 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very low mRNA expression
Manually annotated by BRENDA team
very low mRNA expression
Manually annotated by BRENDA team
very low mRNA expression
Manually annotated by BRENDA team
very low mRNA expression
Manually annotated by BRENDA team
subcuticular skin, lowest mRNA expression in the skin
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
arginine kinase is a key enzyme for energetic balance in invertebrates and plays an important role in invertebrate physiology by buffering the ATP pool accordingly to cellular energy requirements
physiological function
arginine kinase may play an important role in the coupling of energy production and utilization and the immune response in shrimps
additional information
the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, does not interact with arginine in the binary complex. Residue Glu324 is located in the flexible loop 310-320 that covers the active site and only stabilizes in the ternary transition state analogue complex, LvAK-TSAC
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KARG0_PENVA
356
0
40160
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, about, SDS-PAGE
40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, about, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified arginine kinase in binary complex with arginine and in a ternary transition state analogue complex, mixing of 20 mg/ml protein in 10 mM Tris-HCl, pH 8.0, and 1 mM DTT, with with 4 mM L-arginine, 0.001 ml of the solution is then mixed with 0.001 ml of crystallization solution containing 0.2 M sodium acetate, 0.1 M sodium cacodylate, pH 6.5, and 30% w/v PEG 8000, 16°C, 3 weeks. For the ternary complex, the enzyme is cocrystallized with ADP 16 mM, MgCl2 20 mM, L-arginine 40 mM, and NaNO3 75 mM, X-ray diffraction structure determination and analysis at 1.6-1.9 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from abdominal muscles
glutathione Sepharose 4B column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) codon plus cells by prokaryotic expression plasmid pGEX-4T-2 as glutathione S-transferase arginine kinase fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garcia-Orozco, K.D.; Aispuro-Hernandez, E.; Yepiz-Plascencia, G.; Calderon-de-la-Barca, A.M.; Sotelo-Mundo, R.R.
Molecular characterization of arginine kinase, an allergen from the shrimp Litopenaeus vannamei
Int. Arch. Allergy Immunol.
144
23-28
2007
Penaeus vannamei, Penaeus vannamei (Q004B5)
Manually annotated by BRENDA team
Yao, C.L.; Ji, P.F.; Kong, P.; Wang, Z.Y.; Xiang, J.H.
Arginine kinase from Litopenaeus vannamei: cloning, expression and catalytic properties
Fish Shellfish Immunol.
26
553-558
2009
Penaeus vannamei (B0FRF9), Penaeus vannamei
Manually annotated by BRENDA team
Ortea, I.; Canas, B.; Gallardo, J.M.
Mass spectrometry characterization of species-specific peptides from arginine kinase for the identification of commercially relevant shrimp species
J. Proteome Res.
8
5356-5362
2009
Pandalus borealis, Penaeus monodon, Penaeus vannamei, Penaeus notialis, Penaeus indicus, Penaeus merguiensis, Pleoticus muelleri
Manually annotated by BRENDA team
Lopez-Zavala, A.A.; Garcia-Orozco, K.D.; Carrasco-Miranda, J.S.; Sugich-Miranda, R.; Velazquez-Contreras, E.F.; Criscitiello, M.F.; Brieba, L.G.; Rudino-Pinera, E.; Sotelo-Mundo, R.R.
Crystal structure of shrimp arginine kinase in binary complex with arginine-a molecular view of the phosphagen precursor binding to the enzyme
J. Bioenerg. Biomembr.
45
511-518
2013
Penaeus vannamei (Q004B5)
Manually annotated by BRENDA team