Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00810SAICAR synthetase signatures
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00810
Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) catalyzes the seventh step in the de novo purine biosynthetic pathway; the ATP-dependent conversion of 5'-phosphoribosyl-5-aminoimidazole-4-carboxylic acid and aspartic acid to SAICAR [1]. In bacteria (gene purC), fungi (gene ADE1) and plants, SAICAR synthetase is a monofunctional protein; in higher vertebrates it is the N-terminal domain of a bifunctional enzyme that also catalyze phosphoribosylaminoimidazole carboxylase (AIRC) activity.
As signature patterns for SAICAR synthetase, we selected two conserved regions in the central section of this enzyme.
Last update:December 2004 / Pattern and text revised.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Zalkin H. Dixon J.E. |
| Title | De novo purine nucleotide biosynthesis. | |
| Source | Prog. Nucleic Acid Res. Mol. Biol. 42:259-287(1992). | |
| PubMed ID | 1574589 |
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.