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EC Tree
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.
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
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maltodextrin phosphorylase
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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
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-
-
-
phosphorylase, alpha-glucan
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-
-
-
polyphosphorylase
-
-
-
-
potato phosphorylase
-
-
-
-
starch phosphorylase
-
-
-
-
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[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
proposal for catalytic mechanism
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hexosyl group transfer
-
-
-
-
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(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.
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(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
(maltodextrin)n-1 + alpha-D-glucose 1-phosphate
(maltodextrin)n + phosphate
-
maltodextrin phosphorylase is involved in the utilization of maltodextrins
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltotriose + phosphate
maltobiose + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
additional information
?
-
-
phosphorylase GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains
-
-
?
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
maltodextrin phosphorylase, preferred substrate
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r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
preferred substrate of glycogen phosphorylase
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
favoured reaction
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
catalyzes incorporation of glucose into alpha-1,4-glucosidic linkage on exterior chains of primer, glycogen synthesis is preferred
-
r
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(maltodextrin)n-1 + alpha-D-glucose 1-phosphate
(maltodextrin)n + phosphate
-
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
-
-
?
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pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
requirement
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NaF
-
activation, maximal at 200 mM
additional information
-
not activated by Cl-
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4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose
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-
acarbose
-
poor inhibition
ADPglucose
-
competitive inhibition
alpha-D-glucose-1-methylenephosphonate
-
competitive vs. glucose 1-phosphate
Cu2+
-
1 mM, strong inhibition
D-glucose
-
non-competitive
Hg2+
-
1 mM, strong inhibition
iodoacetate
-
weak inhibition
p-chloromercuribenzoate
-
1 mM, 55% inhibition
TDPglucose
-
competitive inhibition
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
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competitive vs. glucose 1-phosphate
glucose 1-phosphate
-
substrate inhibition
glucose 1-phosphate
-
above 2 mM
additional information
-
-
-
additional information
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not inhibited by Mg2+ and Mn2+
-
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5'-AMP
-
activation
5'-AMP
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in both directions
additional information
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not activated by 2'-AMP, 3'-AMP, ADP, adenosine
-
additional information
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not activated by ATP, cAMP
-
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1
glucose 1-phosphate
-
synthesis
1
Glucose-1-phosphate
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-
0.2
maltoheptaose
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phosphorolysis
24.5
maltotriose
-
synthesis
0.5
phosphate
-
phosphorolysis
additional information
additional information
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0.46% glycogen, with AMP, 0.67% glycogen, without AMP
-
3.6
maltotetraose
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synthesis
3.9
maltotetraose
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phosphorolysis
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0.0015
4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose
-
-
0.4
alpha-D-glucose-1-methylenephosphonate
-
-
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6 - 7.5
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approx. half-maximal activity at pH 6.0 and 7.5
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-
Uniprot
brenda
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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
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D339A
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significantly reduced activity
E382A
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significantly reduced activity
E88A
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significantly reduced activity
H341A
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significantly reduced activity
H571L
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significantly reduced activity
T378G
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significantly reduced activity
Y280A
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significantly reduced activity
additional information
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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
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pH 5.3, protamine sulfate, ammonium sulfate, DEAE-cellulose, Sephadex G-200
-
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Chen, G.S.; Segel, I.H.
Purification and properties of glycogen phosphorylase from Escherichia coli
Arch. Biochem. Biophys.
127
175-186
1968
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda