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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Reaction
Reaction on EC 6.3.4.4 - adenylosuccinate synthase
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fully random mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
sequential rapid equilibrium fully random mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
fully random terter mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
random sequential binding mechanism
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
phosphate-binding region of adenylosuccinate synthetase is involved in a conformational change induced by GTP and IMP binding. GTP and IMP binding depend on the presence of the other substrate at the active site of the enzyme
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
sequential mechanism with a fully random order of substrate addition
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GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
rapid equilibrium random AB steady-state ordered C kinetic mechanism
GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
rapid equilibrium random AB steady-state ordered C kinetic mechanism
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