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PROSITE documentation PDOC00095

Phosphorylase pyridoxal-phosphate attachment site





Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PHOSPHORYLASE, PS00102; Phosphorylase pyridoxal-phosphate attachment site  (PATTERN)


Reference

1AuthorsFukui T. Shimomura S. Nakano K.
TitlePotato and rabbit muscle phosphorylases: comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes.
SourceMol. Cell. Biochem. 42:129-144(1982).
PubMed ID7062910



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