Information on EC 2.7.3.1 - guanidinoacetate kinase

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The expected taxonomic range for this enzyme is: Polychaeta

EC NUMBER
COMMENTARY
2.7.3.1
-
RECOMMENDED NAME
GeneOntology No.
guanidinoacetate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + guanidinoacetate = ADP + phosphoguanidinoacetate
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:guanidinoacetate N-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
GK
Namalycastis sp.
Q6AW43
-
glycocyamine kinase
-
-
-
-
glycocyamine kinase
Namalycastis sp.
Q6AW42
-
glycocyamine kinase
Namalycastis sp.
Q6AW43
-
kinase, guanidinoacetate (phosphorylating)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-60-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Namalycastis sp.
-
SwissProt
Manually annotated by BRENDA team
Namalycastis sp.
alpha chain
SwissProt
Manually annotated by BRENDA team
Namalycastis sp.
beta chain
SwissProt
Manually annotated by BRENDA team
three isoforms
-
-
Manually annotated by BRENDA team
Perinereis sp.
polychaete
-
-
Manually annotated by BRENDA team
Polycelis cornuta
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphocreatine
ATP + ?
show the reaction diagram
-
poor substrate
-
-
?
ADP + phosphoguanidinoacetate
ATP + guanidinoacetate
show the reaction diagram
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
Namalycastis sp.
Q6AW42, Q6AW43
0.5% of the activity with glycocyamine
-
-
r
ATP + glycocyamine
ADP + phosphoglycocyamine
show the reaction diagram
Namalycastis sp.
Q6AW42, Q6AW43
-
-
-
r
ATP + guanidine
ADP + phosphoguanidine
show the reaction diagram
Polycelis cornuta, Myxicola infundibulum
-
-
-
-
?
ATP + guanidine
ADP + phosphoguanidine
show the reaction diagram
-
-
-
r
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
Perinereis sp.
-
-
-
?
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
-
-
-
-
-
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
Polycelis cornuta, Myxicola infundibulum
-
-
-
-
?
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
Namalycastis sp.
Q6AW42, Q6AW43
-
-
-
r
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
Perinereis sp.
-
specific for guanidinoacetate, ITP 2%, GTP 0.5% of ATP activity
-
?
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
-
not: arginine, creatine, lombricine
-
-
r
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
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
Perinereis sp.
-
-
-
?
ATP + guanidinoacetate
ADP + phosphoguanidinoacetate
show the reaction diagram
Namalycastis sp.
Q6AW42, Q6AW43
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Perinereis sp.
-
29% of Mg2+-activation
Ca2+
-
slightly
Mg2+
Perinereis sp.
-
5 mM, activation
Mg2+
Namalycastis sp.
Q6AW42, Q6AW43
essential for activation
Mn2+
Perinereis sp.
-
5 mM, activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-guanidinopropionate
Perinereis sp.
-
slight
4-Guanidinobutyrate
Perinereis sp.
-
slight
5,5'-dithiobis(2-nitrobenzoate)
Perinereis sp.
-
-
agmatine
Perinereis sp.
-
-
AMP
Perinereis sp.
-
-
Ca2+
Perinereis sp.
-
-
Chloroacetophenone
-
-
Creatine
Perinereis sp.
-
slight
guanidine
Perinereis sp.
-
slight
Hg2+
Perinereis sp.
-
-
iodoacetamide
Perinereis sp.
-
-
iodoacetic acid
-
-
L-arginine
Perinereis sp.
-
slight
Methylguanine
Perinereis sp.
-
slight
-
N-bromosuccinimide
Perinereis sp.
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
Perinereis sp.
-
-
p-chloromercuribenzoate
-
-
phenylhydrazine
-
inhibits phosphorylation of ADP
Tauroguanine
Perinereis sp.
-
slight
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.8
-
ATP
Perinereis sp.
-
pH 8.1, 25C
0.89
-
ATP
Namalycastis sp.
Q6AW42, Q6AW43
native GK
1.02
-
ATP
Namalycastis sp.
Q6AW42, Q6AW43
recombinant GK beta
3.3
-
ATP
-
-
3.38
-
glycocyamine
Namalycastis sp.
Q6AW42, Q6AW43
recombinant GK beta
4.7
-
glycocyamine
Namalycastis sp.
Q6AW42, Q6AW43
native GK
0.33
-
Guanidinoacetate
-
-
4.1
-
Guanidinoacetate
Perinereis sp.
-
pH 8.1, 25C
6.8
-
phosphoguanidinoacetate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
24
-
glycocyamine
Namalycastis sp.
Q6AW42, Q6AW43
recombinant GK beta
25.3
-
glycocyamine
Namalycastis sp.
Q6AW42, Q6AW43
native GK
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45.3
-
Perinereis sp.
-
pH 8.1, 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
-
phosphorylation of ADP
8.1
-
Perinereis sp.
-
phosphorylation of guanidinoacetate
8.9
-
-
phosphorylation of guanidinoacetate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9
Perinereis sp.
-
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
phosphorylation of guanidinoacetate
35
-
Perinereis sp.
-
phosphorylation of guanidinoacetate
40
-
-
optimum above, phosphorylation of ADP
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16
32
-
less than 50% of maximal activity above and below, phosphorylation of guanidinoacetate
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Namalycastis sp.
Q6AW42, Q6AW43
-
Manually annotated by BRENDA team
Myxicola infundibulum, Polycelis cornuta
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Namalycastis sp.
Q6AW42, Q6AW43
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
Namalycastis sp.
Q6AW42, Q6AW43
SDS-PAGE
79000
-
-
sucrose density gradient centrifugation
80000
-
-
gel filtration
82000
-
-
gel filtration
87500
-
-
amino acid composition
89150
-
-
equilibrium sedimentation centrifugation
90000
-
Perinereis sp.
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
Perinereis sp.
-
1 * 47000 + 1 * 45000, SDS-PAGE
dimer
-
1 * 42200 + 1 * 43800, SDS-PAGE
dimer
Namalycastis sp.
Q6AW42, Q6AW43
alphabeta, 2 * ca. 40000, SDS-PAGE
heterodimer
Namalycastis sp.
Q6AW42
heterodimer with two homologous polypeptide chains, alpha and beta, derived from a common pre mRNA by mutually exclusive N-terminal alternative exons
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the crystal structures of recombinant glycocyamine kinase alphabeta and glycocyamine kinase betabeta from Namalycastis sp. are determined at 2.6 A and 2.4 A resolution, respectively. In addition, the structure of the glycocyamine kinase betabeta is determined at 2.3 A resolution in complex with a transition state analog, Mg2+ ADP-NO3- glycocyamine. In both heterodimeric and homodimeric glycocyamine kinase forms, the conformations of the two N-termini are asymmetric and the asymmetry is different than that reported previously for the homodimeric creatinine kinases from several organisms
Namalycastis sp.
Q6AW42
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9.5
Perinereis sp.
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
Perinereis sp.
-
stable up to
40
-
Perinereis sp.
-
20 min, 4% loss of activity
45
-
Perinereis sp.
-
20 min, 28% loss of activity
50
-
Perinereis sp.
-
inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the recombinant GK alpha enzyme is quite unstable, storage on ice for 4 h caused 10% loss of activity, in contrast GK beta enzyme is stable, the instability of GK alpha is most likely due to its expression as a maltose-binding protein fusion protein
Namalycastis sp.
Q6AW42, Q6AW43
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, ammonium sulfate precipitate
-
-20C, 20 mM Tris-acetate buffer, pH 8.0, 1 mM dithiothreitol, 5% glycerol, several months
Perinereis sp.
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate fractionation, gel filtration on Sephacryl S-200n, and DEAE-5PW ion exchange chromatography
Namalycastis sp.
Q6AW42, Q6AW43
using Ni-NTA chromatography
Namalycastis sp.
Q6AW42
-
Perinereis sp.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
Namalycastis sp.
Q6AW42
expression in Escherichia coli as maltose-binding protein fusion proteins
Namalycastis sp.
Q6AW42, Q6AW43