|PROSITE documentation PDOC00444 [for PROSITE entry PS01266]|
Adenylosuccinate synthetase (EC 188.8.131.52)  plays an important role in purine biosynthesis, by catalyzing the GTP-dependent conversion of IMP and aspartic acid to AMP. Adenylosuccinate synthetase has been characterized from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozymes are present - one involved in purine biosynthesis and the other in the purine nucleotide cycle.
As signature patterns, we selected two conserved regions. The first one is a perfectly conserved octapeptide located in the N-terminal section and which is involved in GTP-binding . The second one includes a lysine residue known  to be essential for the enzyme's activity.Last update:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Wiesmueller L. Wittbrodt J. Noegel A.A. Schleicher M.|
|Source||J. Biol. Chem. 266:2480-2485(1991).|
|2||Authors||Silva M.M. Poland B.W. Hoffman C.R. Fromm H.J. Honzatko R.B.|
|Title||Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli.|
|Source||J. Mol. Biol. 254:431-446(1995).|
|3||Authors||Bouyoub A. Barbier G. Forterre P. Labedan B.|
|Title||The adenylosuccinate synthetase from the hyperthermophilic archaeon Pyrococcus species displays unusual structural features.|
|Source||J. Mol. Biol. 261:144-154(1996).|