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Information on EC 6.3.4.4 - adenylosuccinate synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57981

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.4 adenylosuccinate synthase
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Methanocaldococcus jannaschii
UNIPROT: Q57981 not found.
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
adenylosuccinate synthetase, adssl1, adss1, adenylosuccinate synthase, pfadss, adss2, ampss, succino-amp synthetase, adenylosuccinate synthetase 1, mouse muscle synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Adenylosuccinate synthase
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-
-
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Adenylosuccinate synthetase
AMPSase
IMP--aspartate ligase
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-
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IMP-aspartate ligase
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-
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Succino-AMP synthetase
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-
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Succinoadenylic kinosynthetase
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
rapid equilibrium random AB steady-state ordered C kinetic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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-
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SYSTEMATIC NAME
IUBMB Comments
IMP:L-aspartate ligase (GDP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-57-8
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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
GTP + IMP + L-aspartate
GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
show the reaction diagram
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i.e. adenylosuccinate
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?
GTP + IMP + L-Asp
GDP + phosphate + adenylosuccinate
show the reaction diagram
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-
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-
?
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
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
GTP + IMP + L-aspartate
GDP + phosphate + adenylosuccinate
show the reaction diagram
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first committed step in the de novo biosynthesis of adenosine monophosphate and component of the purine nucleotide cycle
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
requires Mg2+ for catalysis with maximum activity obtained at 15 mM magnesium acetate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenylosuccinate
competitive inhibitor of IMP, noncompetitive inhibitor of GTP and aspartate
AMP
competitive with respect to IMP and noncompetitive with GTP and aspartate
D-fructose 1,6 bisphosphate
competitive with IMP and noncompetitive against GTP
GDP
competitive inhibitor of GTP, noncompetitive inhibitor with IMP and aspartate
GMP
competitive with respect to GTP and noncompetitive with IMP and aspartate
IMP
inhibits the enzyme activity at subsaturating GTP concentrations
N-formyl-N-hydroxyglycine
i.e. hadacidin. competitive inhibitor of aspartate, showed uncompetitive inhibition with IMP and GTP
phosphate
potent inhibitor, biphasic inhibition, competitive with IMP and noncompetitive with GTP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0426
GTP
pH 6.0, 70°C
0.0755
IMP
pH 6.0, 70°C
1.079
L-aspartate
pH 6.0, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45 - 4.2
GTP
0.45 - 4.2
IMP
0.45 - 4.2
L-aspartate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0094 - 0.0429
adenylosuccinate
0.0582 - 0.402
AMP
1.5 - 4.8
D-fructose 1,6 bisphosphate
0.007 - 0.0822
GDP
0.0137 - 0.12
GMP
0.0105 - 0.0269
N-formyl-N-hydroxyglycine
1.9 - 8.3
phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37855
109000
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gel filtration, in the absence of denaturant AdSS elutes as a single peak corresponding to a molecular mass of 109000 Da, which is indicative of dimer-tetramer equilibrium
160000
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gel filtration, in 20 mM Tris-HCl, pH 7.4
38000
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4 * 38000, gel filtration and dynamic light scattering, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
79000
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2 * 79000, gel filtration, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 37855, MALDI mass spectrometric analysis, equilibrium mixture of dimers and tetramers with the tetramer being the catalytically active form. The tetramer dissociates into dimers with a minor increase in ionic strength of the buffer, while the dimer is extremely stable and does not dissociate even at 1.2 M NaCl
tetramer
4 * 37855, MALDI mass spectrometric analysis, equilibrium mixture of dimers and tetramers with the tetramer being the catalytically active form. The tetramer dissociates into dimers with a minor increase in ionic strength of the buffer, while the dimer is extremely stable and does not dissociate even at 1.2 M NaCl
dimer
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2 * 79000, gel filtration, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
tetramer
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4 * 38000, gel filtration and dynamic light scattering, AdSS exhibits dimer-tetramer equilibrium with the equilibrium shifting towards the dimer in the presence of 100 mM NaCl
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of high-resolution vibrational spectral fingerprints of each substrate and intermediate. The bound IMP is distorted toward its N1-deprotonated form even in the absence of any other ligands. Specific interactions between GTP and active-site amino acid residues result in large Raman shifts and contribute substantially to intrinsic binding energy. When both IMP and GTP are simultaneously bound, IMP is converted into an intermediate 6-phosphoryl inosine 5'-monophosphate. The intermediate complex is stable upon binding of the third ligand, L-aspartae analogue hadaicin. In the absence of hadaicin, 6-phosphoryl inosine 5'-monophosphate is quickly released from ADSS, is unstable in solution, and converts back into IMP. Hadaicin allosterically stabilizes ADSS through local conformational rearrangements
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 90
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thermal unfolding of AdSS exhibits a melting temperature of 85°C with the process being only partially reversible, the half life of inactivation is 340 min, 150 min, 110 min, 60 min, 30 min and 15 min at 65, 70, 75, 80, 85 and 90°C, respectively
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
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dramatic loss in secondary structure above 4 M guanidine-HCl with complete loss in secondary structure at 5 M guanidine-HCl
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable without any decrease in activity for at least 6 months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
expressed in Escherichia coli BL21 (DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Honzatko, R.B.; Stayton, M.M.; Fromm, H.J.
Adenylosuccinate synthetase: Recent developments
Adv. Enzymol. Relat. Areas Mol. Biol.
73
57-102
1999
Azotobacter vinelandii, Acidithiobacillus ferrooxidans, Arabidopsis thaliana, Bacillus subtilis, Oryctolagus cuniculus, Dictyostelium discoideum, Escherichia coli, Haemophilus influenzae, Homo sapiens, Leishmania donovani, Methanocaldococcus jannaschii, Mus musculus, Pyrococcus sp., Rattus norvegicus, Schizosaccharomyces pombe, Triticum aestivum, Trypanosoma cruzi, Zea mays, Pyrococcus sp. ST700
Manually annotated by BRENDA team
Mehrotra, S.; Balaram, H.
Methanocaldococcus jannaschii adenylosuccinate synthetase: Studies on temperature dependence of catalytic activity and structural stability
Biochim. Biophys. Acta
1784
2019-2028
2008
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Mehrotra, S.; Balaram, H.
Kinetic characterization of adenylosuccinate synthetase from the thermophilic archaea Methanocaldococcus jannaschii
Biochemistry
46
12821-12832
2007
Methanocaldococcus jannaschii (Q57981), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57981)
Manually annotated by BRENDA team
Karnawat, V.; Mehrotra, S.; Balaram, H.; Puranik, M.
Exquisite modulation of the active site of Methanocaldococcus jannaschii adenylosuccinate synthetase in forward reaction complexes
Biochemistry
55
2491-2499
2016
Methanocaldococcus jannaschii (Q57981), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57981)
Manually annotated by BRENDA team