UniProt functional annotation for P06737



	UniProt functional annotation for P06737

UniProt code: P06737.

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. Interacts with PPP1R3B (By similarity). {ECO:0000250}.

Ptm: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000269|PubMed:10949035}.

Disease: Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected. {ECO:0000269|PubMed:9529348}. 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. Interacts with PPP1R3B (By similarity). {ECO:0000250}.
Ptm:		Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000269\|PubMed:10949035}.
Disease:		Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected. {ECO:0000269\|PubMed:9529348}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the glycogen phosphorylase family. {ECO:0000305}.