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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Escherichia coli and UniProt Accession P00490

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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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This record set is specific for:
Escherichia coli
UNIPROT: P00490
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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
maltodextrin phosphorylase
-
1,4-alpha-glucan phosphorylase
-
-
-
-
alpha-glucan phosphorylase
-
-
-
-
amylopectin phosphorylase
-
-
-
-
amylophosphorylase
-
-
-
-
glucan phosphorylase
-
-
-
-
glucosan phosphorylase
-
-
-
-
glycogen phosphorylase
-
-
-
-
granulose phosphorylase
-
-
-
-
maltodextrin phosphorylase
-
-
-
-
muscle phosphorylase
-
-
-
-
muscle phosphorylase a and b
-
-
-
-
myophosphorylase
-
-
-
-
phosphorylase a
-
-
-
-
phosphorylase, alpha-glucan
-
-
-
-
polyphosphorylase
-
-
-
-
potato phosphorylase
-
-
-
-
starch phosphorylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
show the reaction diagram
proposal for catalytic mechanism
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
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
show the reaction diagram
(maltodextrin)n-1 + alpha-D-glucose 1-phosphate
(maltodextrin)n + phosphate
show the reaction diagram
-
maltodextrin phosphorylase is involved in the utilization of maltodextrins
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
show the reaction diagram
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
maltotriose + phosphate
maltobiose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
show the reaction diagram
additional information
?
-
-
phosphorylase GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains
-
-
?
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
(maltodextrin)n-1 + alpha-D-glucose 1-phosphate
(maltodextrin)n + phosphate
show the reaction diagram
-
maltodextrin phosphorylase is involved in the utilization of maltodextrins
-
r
additional information
?
-
-
phosphorylase GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaF
-
activation, maximal at 200 mM
additional information
-
not activated by Cl-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose
-
-
acarbose
-
poor inhibition
ADPglucose
-
competitive inhibition
Ag+
-
strong inhibition
alpha-Amylose
-
-
-
alpha-D-glucose-1-methylenephosphonate
-
competitive vs. glucose 1-phosphate
arsenate
-
-
beta-Amylose
-
-
Ca2+
-
weak
Cu2+
-
1 mM, strong inhibition
D-glucose
-
non-competitive
Fe2+
-
weak inhibition
gluconolactone
-
-
glucose 1-phosphate
Hg2+
-
1 mM, strong inhibition
iodoacetamide
-
weak
iodoacetate
-
weak inhibition
N-ethylmaleimide
-
weak
p-chloromercuribenzoate
-
1 mM, 55% inhibition
TDPglucose
-
competitive inhibition
UDPglucose
-
-
Zn2+
-
strong inhibition
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
-
competitive vs. glucose 1-phosphate
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-AMP
CNO-
-
slight activation
Na2SO4
-
activation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
glucose 1-phosphate
-
synthesis
1
Glucose-1-phosphate
-
-
0.2
maltoheptaose
-
phosphorolysis
3.6 - 3.9
maltotetraose
24.5
maltotriose
-
synthesis
0.5
phosphate
-
phosphorolysis
additional information
additional information
-
0.46% glycogen, with AMP, 0.67% glycogen, without AMP
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose
-
-
0.7
ADP-glucose
-
-
0.4
alpha-D-glucose-1-methylenephosphonate
-
-
0.5
arsenate
-
-
0.9
gluconolactone
-
-
2.5
glucose
-
-
1
TDP-glucose
-
-
2
UDP-glucose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 6.9
-
glycogen
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
approx. half-maximal activity at pH 6.0 and 7.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ternary complexes of maltodextrin phosphorylase with natural oligosaccharide and phosphate mimicking anions: nitrate, sulphate and vanadate. Electron density maps obtained from crystals grown in presence of Al(NO3)3 show a nitrate ion instead of the expected AlF4- in the catalytic site. The trigonal NO3- is coplanar with the Arg569 guanidinium group and mimics three of the four oxygen atoms of phosphate. The ternary complex with sulphate shows a partial occupancy of the anionic site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D339A
-
significantly reduced activity
E382A
-
significantly reduced activity
E88A
-
significantly reduced activity
H341A
-
significantly reduced activity
H571L
-
significantly reduced activity
T378G
-
significantly reduced activity
Y280A
-
significantly reduced activity
additional information
-
phosphorylase deletion mutants totally lack enzymic activity. Both glycogen contnent and rates of intracellular glycogen levels are severalfold higher than those of wild-type. Mutants accumulate longer external chains in the polysaccharide
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH 5.3, protamine sulfate, ammonium sulfate, DEAE-cellulose, Sephadex G-200
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, G.S.; Segel, I.H.
Purification and properties of glycogen phosphorylase from Escherichia coli
Arch. Biochem. Biophys.
127
175-186
1968
Escherichia coli
Manually annotated by BRENDA team
Boeck, B.; Schinzel, R.
Purification and characterization of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus
Eur. J. Biochem.
239
150-155
1996
Escherichia coli, Thermus thermophilus
Manually annotated by BRENDA team
Watson, K.A.; McCleverty, C.; Geremia, S.; Cottaz, S.; Driguez, H.; Johnson, L.N.
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question
EMBO J.
18
4619-4632
1999
Escherichia coli
Manually annotated by BRENDA team
Schinzel, R.; Nidetzky, B.
Bacterial alpha-glucan phosphorylases
FEMS Microbiol. Lett.
171
73-79
1999
Corynebacterium callunae, Escherichia coli, Thermus thermophilus, Klebsiella pneumoniae, Streptococcus salivarius
Manually annotated by BRENDA team
Geremia, S.; Campagnolo, M.; Schinzel, R.; Johnson, L.N.
Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase
J. Mol. Biol.
322
413-423
2002
Escherichia coli (P00490), Escherichia coli
Manually annotated by BRENDA team
Alonso-Casajus, N.; Dauvillee, D.; Viale, A.M.; Munoz, F.J.; Baroja-Fernandez, E.; Moran-Zorzano, M.T.; Eydallin, G.; Ball, S.; Pozueta-Romero, J.
Glycogen phosphorylase, the product of the glgP Gene, catalyzes glycogen breakdown by removing glucose units from the nonreducing ends in Escherichia coli
J. Bacteriol.
188
5266-5272
2006
Escherichia coli
Manually annotated by BRENDA team
Campagnolo, M.; Campa, C.; Zorzi, R.D.; Wuerges, J.; Geremia, S.
X-ray studies on ternary complexes of maltodextrin phosphorylase
Arch. Biochem. Biophys.
471
11-19
2008
Escherichia coli (P00490)
Manually annotated by BRENDA team