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2.4.1.1 |
Description |
Phosphorylase |
Alternative names |
Muscle phosphorylase A and B; Amylophosphorylase; Polyphosphorylase. |
Catalyzed reaction |
{(1,4)-alpha-D-glucosyl}(N) + phosphate = {(1,4)-alpha-D-glucosyl}(N-1) + alpha-D-glucose 1-phosphate. |
Cofactor |
Pyridoxal-phosphate. |
Comments |
-!- The recommended name should be qualified in each instance by adding the name of the natural substance, e.g. maltodextrin phosphorylase, starch phosphorylase, glycogen phosphorylase. |
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Phosphorylases are unusual PLP-dependent enzymes, in that the reactive part of the cofactor is not the aromatic aldehyde moiety, but rather the phosphate group, which functions as a general acid/base catalyst. |
Diseases |
Glycogen storage diseases V and VI. |
Prosite |
PROSITE; PDOC00095; |
PDB |
1GPB; 7GPB; 1ABB; 1AHP; 1L5W; 1LWN; |
Organisms |
-Eubacteria -Archea -Plants -Fungi -Metazoa -Human |
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Links |
Enzyme (activities) 2.4.1.1
BRENDA (activities) 2.4.1.1
KEGG (pathways) 2.4.1.1
PLPMDB (PLP mutants) 2.4.1.1
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References |
Articles on 2.4.1.1 |
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last changed |
2018/05/24 13:30 |
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