Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.3.3 - arginine kinase and Organism(s) Penaeus japonicus and UniProt Accession P51545

for references in articles please use BRENDA:EC2.7.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Penaeus japonicus
UNIPROT: P51545 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Penaeus japonicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
arginine kinase, argk, arginine phosphokinase, pyak3, tcak1, mnak2, tcak2, tbak3, pyak2, pyak4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine 5'-triphosphate-arginine phosphotransferase
-
-
-
-
adenosine 5'-triphosphate: L-arginine phosphotransferase
-
-
-
-
AK
-
-
-
-
arginine phosphokinase
-
-
-
-
ArgK
-
-
-
-
ATP:L-arginine N-phosphotransferase
-
-
-
-
kinase, arginine (phosphorylating)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ATP:L-arginine Nomega-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-70-4
-
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 + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
4 mM, activation
Co2+
-
4 mM, activation
Fe2+
-
4 mM, activation
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
synthesis of ATP
9
-
synthesis of N-phospho-L-arginine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 60
-
10°C: about 50% of maximal activity, 60°C: about 60% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
arginine kinase up-regulation under hypoxia may indicate a provision for oxygen re-supply after anaerobiosis
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KARG_PENJP
355
0
39991
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
10 min, stable up to
25
-
10 min, inactivation above
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
more stable in 100 mM Tris-HCl buffer at pH 8.0 than in 100 mM phosphate buffer at pH 7.0
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HCl buffer, pH 8.5, activity gradually decreases, but can be restored by addition of 1 mM 2-mercaptoethanol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the His6-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Livera, W.C.D.; Shimizu, C.
Comparison and characterization of arginine kinases purified from the prawn Penaeus japonicus (Kurumaebi) and the swimming crab Portunus trituberculatus
Agric. Biol. Chem.
53
2377-2386
1989
Penaeus japonicus, Portunus trituberculatus
-
Manually annotated by BRENDA team
Abe, H.; Hirai, S.; Okada, S.
Metabolic responses and arginine kinase expression under hypoxic stress of the kuruma prawn Marsupenaeus japonicus
Comp. Biochem. Physiol. A
146A
40-46
2007
Penaeus japonicus (P51545)
-
Manually annotated by BRENDA team
Wang, J.; Yang, K.; Zhang, X.
Characterization of the interaction between arginine kinase and siRNA
Mar. Biotechnol.
15
368-374
2013
Penaeus japonicus (P51545)
Manually annotated by BRENDA team