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Information on EC 2.7.3.3 - arginine kinase and Organism(s) Limulus polyphemus and UniProt Accession P51541

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Limulus polyphemus
UNIPROT: P51541 not found.
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The taxonomic range for the selected organisms is: Limulus polyphemus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
arginine kinase, argk, arginine phosphokinase, tcak1, mnak2, tcak2, pyak3, pyak4, tbak3, pyak2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP: L-arginine phosphotransferase
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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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-
-
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arginine phosphokinase
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-
-
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ArgK
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-
-
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ATP:L-arginine N-phosphotransferase
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-
-
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kinase, arginine (phosphorylating)
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
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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 + Nomega-phospho-L-Arg
show the reaction diagram
ADP + Nomega-phospho-L-arginine
ATP + L-arginine
show the reaction diagram
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-
-
-
?
ATP + L-Arg
ADP + Nomega-phospho-L-Arg
show the reaction diagram
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-
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required, bound to ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.26
ADP
0.63 - 1.45
N5-(N-phosphonocarbamimidoyl)-L-ornithine
additional information
additional information
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-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 140
ADP
0.27 - 140
N5-(N-phosphonocarbamimidoyl)-L-ornithine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
268.6
recombinant wild type enzyme, pH and temperature not specified in the publication
53.78
mutant enzyme R330K, pH and temperature not specified in the publication
0.245
-
homogenous muscle enzyme
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_LIMPO
357
0
40239
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40238
-
x * 40238, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40238, calculation from nucleotide sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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polyethylene glycol precipitation of recombinant enzyme. Crystallization as a transition state analog
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R330K
the mutant enzyme is more susceptible to oxidation than the wild type enzyme and shows 20% of wild type activity
E225A
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turnover number is 0.03% of the wild-type value
E225D
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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
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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
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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
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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
E314Q
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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
R312G/E314V/H315D/E317A/E319V
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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
additional information
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional crystal structure of an arginine kinase transition-state analogue complex refined at 1.2 A resolution
recombinant enzyme from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta cells
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, G.; Parthasarathy, G.; Somasundaram, T.; Ables, A.; Roy, L.; Strong, S.J.; Ellington, W.R.; Chapman, M.S.
Expression, purification from inclusion bodies, and crystal characterization of a transition state analog complex of arginine kinase: a model for studying phosphagen kinases
Protein Sci.
6
444-449
1997
Limulus polyphemus
Manually annotated by BRENDA team
Strong, S.J.; Ellington, W.R.
Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues
Biochim. Biophys. Acta
1246
197-200
1995
Limulus polyphemus
Manually annotated by BRENDA team
Strong, S.J.; Ellington, W.R.
Expression of horseshoe crab arginine kinase in Escherichia coli and site-directed mutations of the reactive cysteine peptide
Comp. Biochem. Physiol. B
113
809-816
1996
Limulus polyphemus
Manually annotated by BRENDA team
Yousef, M.S.; Fabiola, F.; Gattis, J.L.; Somasundaram, T.; Chapman, M.S.
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights
Acta Crystallogr. Sect. D
58
2009-2017
2002
Limulus polyphemus (P51541)
Manually annotated by BRENDA team
Pruett, P.S.; Azzi, A.; Clark, S.A.; Yousef, M.S.; Gattis, J.L.; Somasundaram, T.; Ellington, W.R.; Chapman, M.S.
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
J. Biol. Chem.
278
26952-26957
2003
Limulus polyphemus
Manually annotated by BRENDA team
Clark, S.A.; Davulcu, O.; Chapman, M.S.
Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs
Biochem. Biophys. Res. Commun.
427
212-217
2012
Limulus polyphemus (P51541), Limulus polyphemus
Manually annotated by BRENDA team
Wang, W.D.; Wang, J.S.; Shi, Y.L.; Zhang, X.C.; Pan, J.C.; Zou, G.L.
Mutation of residue arginine 330 of arginine kinase results in the generation of the oxidized form more susceptible
Int. J. Biol. Macromol.
54
238-243
2013
Limulus polyphemus (P51541)
Manually annotated by BRENDA team