Names & Taxonomy

Uniprot ID:
P06737
Entry Name:
PYGL_HUMAN
Status:
reviewed
Protein Names:
Glycogen phosphorylase, liver form (EC 2.4.1.1)
Gene Names:
PYGL
Gene Names Primary:
PYGL
Organism:
Homo sapiens (Human)

Structure

Length:
847
Sequence:
MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFPKDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFVPRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEAYVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNESNKVNGN
Proteomes:
UP000005640

Function

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:
((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
Cofactor:
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Enzyme Regulation:
ENZYME 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.
Cross Reference Drug Bank:
DB00131
Gene Ontology Go:
cytoplasm
cytosol
extracellular exosome
plasma membrane
AMP binding
ATP binding
bile acid binding
drug binding
glucose binding
glycogen phosphorylase activity
protein homodimerization activity
purine nucleobase binding
pyridoxal phosphate binding
vitamin binding
5-phosphoribose 1-diphosphate biosynthetic process
carbohydrate metabolic process
glucose homeostasis
glucose metabolic process
glycogen catabolic process
glycogen metabolic process
necroptotic process
small molecule metabolic process
Gene Ontology Biological Process:
5-phosphoribose 1-diphosphate biosynthetic process
carbohydrate metabolic process
glucose homeostasis
glucose metabolic process
glycogen catabolic process
glycogen metabolic process
necroptotic process
small molecule metabolic process
Gene Ontology Molecular Function:
AMP binding
ATP binding
bile acid binding
drug binding
glucose binding
glycogen phosphorylase activity
protein homodimerization activity
purine nucleobase binding
pyridoxal phosphate binding
vitamin binding
Gene Ontology Cellular Component:
cytoplasm
cytosol
extracellular exosome
plasma membrane
Keywords:
3D-structure
Acetylation
Allosteric enzyme
Alternative splicing
Carbohydrate metabolism
Complete proteome
Disease mutation
Glycogen metabolism
Glycogen storage disease
Glycosyltransferase
Nucleotide-binding
Phosphoprotein
Polymorphism
Pyridoxal phosphate
Reference proteome
Transferase
Interacts With:
P11216

Publication

PubMed ID:
2877458 9536091 9529348 14702039 12508121 15489334 3509980 19413330 21269460 22814378 24275569 10980448 10949035 12204691