6.3.2.6: phosphoribosylaminoimidazolesuccinocarboxamide synthase This is an abbreviated version! For detailed information about phosphoribosylaminoimidazolesuccinocarboxamide synthase, go to the full flat file .
Reaction
ATP +
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate +
L-aspartate =
ADP +
phosphate +
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
Synonyms 4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide synthetase, 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase, 5-Aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase, ade5, AIRc-SAICARs, ATPase, BaPurC, CCM_04437, MjSS, More, N-(5-Amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5´-phosphate synthetase, PAICS, PH0239, PH0239 protein, phosphoribosylaminoimidazole succinocarboxamide synthetase, phosphoribosylaminoimidazole-succinocarboxamide synthase, phosphoribosylaminoimidazole-succinocarboxamide synthetase, Phosphoribosylaminoimidazolesuccinocarboxamide synthetase, PhSS, PurC, PurC gene product, PurCE, SAICAR synthase, SAICAR synthetase, spPurC, Succino-AICAR synthetase, Synthetase, phosphoribosylaminoimidazolesuccinocarboxamide, VEG286A, Vegetative protein 286A
ECTree
Temperature Stability
Temperature Stability on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase
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additional information
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27-100°C, structure-thermostability molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
additional information
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27-100°C, structure-thermostability molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
additional information
-
27-100°C, structure-thermostability molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
additional information
delineation of the mesophilic (Escherichia coli, Ehrlichia chaffeensis), thermophilic (Geobacillus kaustophilus), and hyperthermophilic (Methanocaldococcus jannaschii, Pyrococcus horikoshii) proteins on the basis of their thermal stability by studying their dynamic aspects at 27°C and 60°C using molecular dynamics
additional information
delineation of the mesophilic (Escherichia coli, Ehrlichia chaffeensis), thermophilic (Geobacillus kaustophilus), and hyperthermophilic (Methanocaldococcus jannaschii, Pyrococcus horikoshii) proteins on the basis of their thermal stability by studying their dynamic aspects at 27°C and 60°C using molecular dynamics