UniProt functional annotation for P11217



	UniProt functional annotation for P11217

UniProt code: P11217.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Catalytic activity: Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;

Cofactor: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;

Activity regulation: Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.

Subunit: Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

Ptm: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000269|PubMed:1150650}.

Disease: Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria. {ECO:0000269|PubMed:10382911, ECO:0000269|PubMed:10382912, ECO:0000269|PubMed:10417800, ECO:0000269|PubMed:10590419, ECO:0000269|PubMed:10681080, ECO:0000269|PubMed:10714589, ECO:0000269|PubMed:10899452, ECO:0000269|PubMed:11706962, ECO:0000269|PubMed:12031624, ECO:0000269|PubMed:7603523, ECO:0000269|PubMed:8316268, ECO:0000269|PubMed:8535454, ECO:0000269|PubMed:9506549}. Note=The disease is caused by variants affecting the gene represented in this entry.

Similarity: Belongs to the glycogen phosphorylase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.


Catalytic activity:		Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
Cofactor:		Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Activity regulation:		Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.
Subunit:		Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.
Ptm:		Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000269\|PubMed:1150650}.
Disease:		Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria. {ECO:0000269\|PubMed:10382911, ECO:0000269\|PubMed:10382912, ECO:0000269\|PubMed:10417800, ECO:0000269\|PubMed:10590419, ECO:0000269\|PubMed:10681080, ECO:0000269\|PubMed:10714589, ECO:0000269\|PubMed:10899452, ECO:0000269\|PubMed:11706962, ECO:0000269\|PubMed:12031624, ECO:0000269\|PubMed:7603523, ECO:0000269\|PubMed:8316268, ECO:0000269\|PubMed:8535454, ECO:0000269\|PubMed:9506549}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the glycogen phosphorylase family. {ECO:0000305}.