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Information on EC 2.7.3.3 - arginine kinase and Organism(s) Anthopleura japonica and UniProt Accession O15992

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This record set is specific for:
Anthopleura japonica
UNIPROT: O15992 not found.
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The taxonomic range for the selected organisms is: Anthopleura japonica
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
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-
-
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adenosine 5'-triphosphate: L-arginine phosphotransferase
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-
-
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AK
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-
-
-
arginine phosphokinase
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-
-
-
ArgK
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-
-
-
ATP:L-arginine N-phosphotransferase
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-
-
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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
-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
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-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
Mg2+
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activates at concentrations greater than 1 mM, maximal effect at 1.5 mM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
129
ATP
recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains
129
L-Arg
recombinant wild-type enzyme with MBP tag
89 - 678
L-Arg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KARG_ANTJA
715
0
80024
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
1 * 40000, SDS-PAGE
79933
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1 * 79933, calculation from nucleotide sequence
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D62E
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
D62G
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
Y68G
-
the mutation in domain 1 or 2 leads to almost no catalytic activity
additional information
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
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
expressed in Escherichia coli BL21 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, T.; Kawasaki, Y.; Furukohri, T.
Evolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus
Biochem. J.
328
301-306
1997
Anthopleura japonica
Manually annotated by BRENDA team
Tada, H.; Nishimura, Y.; Suzuki, T.
Cooperativity in the two-domain arginine kinase from the sea anemone Anthopleura japonicus
Int. J. Biol. Macromol.
42
46-51
2008
Anthopleura japonica (O15992), Anthopleura japonica
Manually annotated by BRENDA team
Tada, H.; Suzuki, T.
Cooperativity in the two-domain arginine kinase from the sea anemone Anthopleura japonicus. II. Evidence from site-directed mutagenesis studies
Int. J. Biol. Macromol.
47
250-254
2010
Anthopleura japonica
Manually annotated by BRENDA team