PROSITE documentation PDOC00444Adenylosuccinate synthetase signatures
Adenylosuccinate synthetase (EC 6.3.4.4) [1] 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 [2]. The second one includes a lysine residue known [2] 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). | |
| PubMed ID | 7490761 |
| 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). | |
| PubMed ID | 8757283 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)