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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Dictyostelium discoideum

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.1 glycogen phosphorylase
IUBMB Comments
This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.
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Dictyostelium discoideum
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The taxonomic range for the selected organisms is: Dictyostelium discoideum
The enzyme appears in selected viruses and cellular organisms
Synonyms
glycogen phosphorylase, phosphorylase a, phosphorylase b, myophosphorylase, muscle phosphorylase, glycogen phosphorylase b, glycogen phosphorylase a, muscle glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-glucan phosphorylase
-
-
-
-
alpha-glucan phosphorylase
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-
-
-
amylopectin phosphorylase
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-
-
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amylophosphorylase
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-
-
-
glucan phosphorylase
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-
-
-
glucosan phosphorylase
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-
-
-
glycogen phosphorylase
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-
-
-
granulose phosphorylase
-
-
-
-
maltodextrin phosphorylase
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-
-
-
muscle phosphorylase
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-
-
-
muscle phosphorylase a and b
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-
-
-
myophosphorylase
-
-
-
-
phosphorylase a
-
-
-
-
phosphorylase, alpha-glucan
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-
-
-
polyphosphorylase
-
-
-
-
potato phosphorylase
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-
-
-
starch phosphorylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:phosphate alpha-D-glucosyltransferase
This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.
CAS REGISTRY NUMBER
COMMENTARY hide
9035-74-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycogen + glucose 1-phosphate
glycogen + phosphate
show the reaction diagram
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
show the reaction diagram
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key step in cellular differentiation of Dictyostelium discoideum
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADPglucose
-
competitive inhibition
AMP
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isozyme a; weak
GDPglucose
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0.05 mM, 50% inhibition, competitive inhibition of phosphorolysis
glucose 1-phosphate
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kinetics
high salt concentration
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-
-
KCl
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80 mM, 50% loss of activity, 200 mM, 90% loss of activity
UDPglucose
-
kinetics
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-AMP
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 55
phosphate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
glucose 1-phosphate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
isozyme a, 2-(N-morpholino)ethanesulfonic acid preferred to imidazole buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 7.2
-
approx. half-maximal activity at pH 5.8 and 7.2, a-isozyme
5.8 - 7.6
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approx. half-maximal activity at pH 5.8 and 7.6, b-isozyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18 - 35
-
approx. half-maximal activity at 18°C and 35°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHS1_DICDI
853
0
98277
Swiss-Prot
other Location (Reliability: 3)
PHS2_DICDI
993
0
113104
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95000
-
2 * 95000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
-
inactivation above
50
-
inactivation within 5 min, isozyme b
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze-thawing inactivates
-
Streptomycin sulfate or ammonium sulfate precipitation inactivates b-, not a-isozyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
7°C, isozyme b, inactivation within 48 h, isozyme a: at least 48 h, in crude extract
-
glycerol stabilizes purified enzyme during storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozymes a, streptomycin sulfate, ammonium sulfate, 50°C, DE52-cellulose, aminobutyl-agarose, Sephacryl S-300, isoenzyme b, DE52-cellulose, 5'-AMP-Sepharose
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Streptomycin sulfate, ammonium sulfate, heat, DEAE-cellulose, Sepharose 2B, preparative gel electrophoresis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thomas, D.A.; Wright, B.E.
Glycogen phosphorylase in Dictyostelium discoideum. I. Purification and properties of the enzyme
J. Biol. Chem.
254
1253-1257
1976
Dictyostelium discoideum
-
Manually annotated by BRENDA team
Cloutier, M.J.; Rutherford, C.L.
Glycogen phosphorylase in Dictyostelium. Developmental regulation of two forms and their physical and kinetic properties
J. Biol. Chem.
262
9486-9493
1987
Dictyostelium discoideum
Manually annotated by BRENDA team