6.3.4.4: adenylosuccinate synthase
This is an abbreviated version!
For detailed information about adenylosuccinate synthase, go to the full flat file.
Word Map on EC 6.3.4.4
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6.3.4.4
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purine
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gtp
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inosine
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hadacidin
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hypoxanthine
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formycin
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adenylosuccinase
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alanosine
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medicine
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saicar
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synthesis
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agriculture
- 6.3.4.4
- purine
- gtp
- inosine
- hadacidin
- hypoxanthine
- formycin
- adenylosuccinase
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alanosine
- medicine
-
saicar
- synthesis
- agriculture
Reaction
Synonyms
adenosylsuccinate synthase, adenosylsuccinate synthetase, adenylo-succinate synthetase, Adenylosuccinate synthase, Adenylosuccinate synthetase, adenylosuccinate synthetase 1, AdSS, AdSS1, AdSS2, AdSSL1, AMPSase, AMPsS, Arabdss, AS-synthetase, ASS, IMP--aspartate ligase, IMP-aspartate ligase, mouse muscle synthetase, PfAdSS, purA, Succino-AMP synthetase, Succinoadenylic kinosynthetase, Wheatadss
ECTree
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Subunits
Subunits on EC 6.3.4.4 - adenylosuccinate synthase
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dimer
homodimer
monomer
tetramer
additional information
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
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
dimer
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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
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dimer
1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
dimer
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1 * 80000, the enzyme mainly exists as dimer in solution, SDS-PAGE
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dimer
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2 * 47000, sedimentation equilibrium analysis in presence of 6 M guanidine-HCl
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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
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
tetramer
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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
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conserved arginine residue R155 is involved in dimer crosstalk and interacts with IMP in the active site of the symmetry related subunit
additional information
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conserved arginine residue R155 is involved in dimer crosstalk and interacts with IMP in the active site of the symmetry related subunit