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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Aquifex aeolicus and UniProt Accession O66932
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2.4.1.1 glycogen phosphorylaseIUBMB 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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Word Map
- 2.4.1.1
- amp
-
glycogenolysis
- hepatocytes
- mcardle
- glucagon
- glucose-6-phosphatase
- pyridoxal
- hexokinase
- 6-phosphate
- creatine
- epinephrine
- myopathy
- phosphorylases
-
phosphofructokinase
- intolerance
-
gluconeogenesis
- glucose-1-phosphate
-
phosphorolysis
- bb
- troponins
-
antidiabetic
- sarcoplasm
- maltodextrins
-
amp-dependent
- isoproterenol
- vasopressin
-
gluconeogenic
- phenylephrine
- glucokinase
- rhabdomyolysis
- myoglobinuria
- pp1
-
beta-adrenergic
- adrenaline
- phosphatase-1
- phosphocreatine
- phosphoglucomutase
-
debranching
- soleus
-
glucose-6-p
- adp-glucose
- g6pase
-
glucagon-stimulated
- inhibitor-2
-
2,6-bisphosphate
-
glycogenesis
-
t-state
- amylose
- biotechnology
- amyloplasts
- medicine
-
heart-type
- agriculture
- analysis
- synthesis
- drug development
The taxonomic range for the selected organisms is: Aquifex aeolicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glycogen phosphorylase, phosphorylase a, phosphorylase b, myophosphorylase, muscle phosphorylase, glycogen phosphorylase b, glycogen phosphorylase a, muscle glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
ORGANISM
UNIPROT
LITERATURE
[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
sequential random bi bi mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
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
9035-74-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
-
-
-
r
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltopentaose + alpha-D-glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
-
-
-
r
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
maltotriose is the smallest substrate accepted for the synthetic reaction direction, maltotetraose is the smallest substrate accepted for the phosphorolytic reaction direction
-
-
r
additional information
?
-
maltotriose is the smallest substrate accepted for the synthetic reaction direction, maltotetraose is the smallest substrate accepted for the phosphorolytic reaction direction
-
-
?
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
polysaccharide substrate is glycogen, mobilization of glucose 1-phosphate as readily useable energy source
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
polysaccharide substrates are glycogen and starch, phosphorolysis is the preferred reaction
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
polysaccharide substrate is glycogen, mobilization of glucose 1-phosphate as readily useable energy source
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics, forward and reverse reaction, recombinant enzyme
-
0.19
maltoheptaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.38
maltoheptaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.18
maltohexaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.3
maltohexaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.17
maltopentaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.28
maltopentaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.3
maltotetraose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.55
maltotetraose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.3
maltoheptaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
4.4
maltoheptaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
2.7
maltohexaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
4.1
maltohexaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
2.2
maltopentaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
5.4
maltopentaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.76
maltotetraose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
x * 80000, recombinant His-tagged enzyme, SDS-PAGE, x * 81981, sequence calculation
81981
x * 80000, recombinant His-tagged enzyme, SDS-PAGE, x * 81981, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 80000, recombinant His-tagged enzyme, SDS-PAGE, x * 81981, sequence calculation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
recombinant enzyme, stable, 61% remaining activity at 70°C and pH 10.4
659735
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli 6.3fold to homogeneity by heat treatment at 70°C and nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene glgP, DNA sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhuiyan, S.H.; Rus'd, A.A.; Kitaoka, M.; Hayashi, K.
Characterization of a hyperthermostable glycogen phosphorylase from Aquifex aeolicus expressed in Escherichia coli
J. Mol. Catal. B
22
173-180
2003
Aquifex aeolicus (O66932)
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EXTERNAL LINKS (specific for EC-Number 2.4.1.1)
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