![]() |
|
|||||||
| PROSITE documentation PDOC00096 |
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:
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].
In position 11 of the pattern most of these enzymes have Gly.
November 1997 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
| PUR_PYR_PR_TRANSFER, PS00103; Purine/pyrimidine phosphoribosyl transferases signature (PATTERN) | ||||||
| ||||||
| Matching PDB structures: 1A95 1A96 1A97 1AO0 ... [ALL] |
| 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 copyright. It is produced by the Swiss Institute of Bioinformatics (SIB). There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to license@isb-sib.ch or see: http://www.expasy.org/prosite/prosite_license.htm.