PROSITE documentation PDOC00095Phosphorylase pyridoxal-phosphate attachment site
Phosphorylases (EC 2.4.1.1) [1] are important allosteric enzymes in carbohydrate metabolism. They catalyze the formation of glucose 1-phosphate from polyglucose such as glycogen, starch or maltodextrin. Enzymes from different sources differ in their regulatory mechanisms and their natural substrates. However, all known phosphorylases share catalytic and structural properties. They are pyridoxal-phosphate dependent enzymes; the pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved and can be used as a signature pattern to detect this class of enzymes.
Last update:November 1997 / Pattern and text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Fukui T. Shimomura S. Nakano K. |
Title | Potato and rabbit muscle phosphorylases: comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes. | |
Source | Mol. Cell. Biochem. 42:129-144(1982). | |
PubMed ID | 7062910 |
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)