 |
|
| PROSITE documentation PDOC00096 [for PROSITE entry PS00103] |
Purine/pyrimidine phosphoribosyl transferases signature
Phosphoribosyltransferases (PRT) are enzymes that catalyze the synthesis of β-n-5'-monophosphates from phosphoribosylpyrophosphate (PRPP) and an enzyme specific amine. A number of PRT's are involved in the biosynthesis of purine, pyrimidine, and pyridine nucleotides, or in the salvage of purines and pyrimidines. These enzymes are:
- Adenine phosphoribosyltransferase (EC 2.4.2.7) (APRT), which is involved in purine salvage.
- Hypoxanthine-guanine or hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) (HGPRT or HPRT), which are involved in purine salvage.
- Orotate phosphoribosyltransferase (EC 2.4.2.10) (OPRT), which is involved in pyrimidine biosynthesis.
- Amido phosphoribosyltransferase (EC 2.4.2.14), which is involved in purine biosynthesis.
- Xanthine-guanine phosphoribosyltransferase (EC 2.4.2.22) (XGPRT), which is involved in purine salvage.
In the sequence of all these enzymes there is a small conserved region which may be involved in the enzymatic activity and/or be part of the PRPP binding site [1].
Note:In position 11 of the pattern most of these enzymes have Gly.
Last update:November 1997 / Pattern and text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Hershey H.V. Taylor M.W. |
| Title | Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. | |
| Source | Gene 43:287-293(1986). | |
| PubMed ID | 3527873 |
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)