poly((1,4)-alpha-glycosyl) glycogenin-1 + n orthophosphate => glycogenin-1 + n D-glucose 1-phosphate [PYGM,PYGB]

Stable Identifier
R-HSA-453358
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
The PYGM and PYGB forms of glycogen phosphorylase catalyze the reaction of orthophosphate and poly((1,4) alpha glucosyl) glycogenin-1 to form D-glucose 1-phosphate and glycogenin-1. This reaction occurs on the surfaces of cytosolic glycogen granules. The phosphorylated forms of PYGM and PYGB dimers (a form) are catalytically active; the non-phosphorylated dimers (b form) become active when complexed with AMP. In the body, this reaction takes place in tissues other than the liver where its sensitivity to AMP allows glucose mobilization in response to acute energy needs of the individual cell, and hormonally mediated phosphorylation can stimulate increased glucose production, still for use by the individual producing cell, in response to stress signals. These reactions have not been characterized in detail but are inferred to occur from the very close similarity among PGYM, PGYB, and PGYL (Newgard et al. 1989; Rath et al. 2000).
Literature References
PubMed ID Title Journal Year
10949035 Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core

Danley, DE, Mansour, MN, Ammirati, M, Pandit, J, Schulte, GK, LeMotte, PK, Wasilko, DJ, Fennell, KF, Rath, VL, Hynes, TR

Mol Cell 2000
2667896 The family of glycogen phosphorylases: structure and function

Hwang, PK, Newgard, CB, Fletterick, RJ

Crit Rev Biochem Mol Biol 1989
Participants
Participates
Catalyst Activity

glycogen phosphorylase activity of active PYGM and PYGB dimers [cytosol]

Inferred From
Authored
Created
Cite Us!