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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Oryza sativa
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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: Oryza sativa
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
-
-
-
-
Pho1
phosphorylase a
-
-
-
-
phosphorylase, alpha-glucan
-
-
-
-
polyphosphorylase
-
-
-
-
potato phosphorylase
-
-
-
-
starch phosphorylase
alpha-glucan phosphorylase
-
-
-
-
starch phosphorylase
-
-
-
-
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
-
low activity
-
-
r
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
-
low activity
-
-
r
maltononaose + alpha-D-glucose 1-phosphate
maltodecaose + phosphate
-
low activity
-
-
r
maltooctaose + alpha-D-glucose 1-phosphate
maltononaose + phosphate
-
low activity
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is starch, phosphorolysis is the physiologic reaction of the starch degrading enzyme
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrates are soluble starch and Zulkowsky soluble starch, amylopectin, glycogen, and dextrin, amyylopectin is the best substrate
-
-
r
[(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
usage of four different assay methods
-
-
r
additional information
?
-
-
substrate specificity, no or nearly no activity with glucose, maltose, and maltotriose, overview
-
-
?
additional information
?
-
-
enzyme is involved in starch degradation during submergence stress in rice plants
-
-
?
additional information
?
-
Pho1 not only degrades maltohexaose but also extends them to synthesize longer malto-oligosaccharides, production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
-
-
?
additional information
?
-
-
Pho1 not only degrades maltohexaose but also extends them to synthesize longer malto-oligosaccharides, production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
-
-
?
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 starch, phosphorolysis is the physiologic reaction of the starch degrading enzyme
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
additional information
?
-
-
enzyme is involved in starch degradation during submergence stress in rice plants
-
-
?
additional information
?
-
Pho1 not only degrades maltohexaose but also extends them to synthesize longer malto-oligosaccharides, production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
-
-
?
additional information
?
-
-
Pho1 not only degrades maltohexaose but also extends them to synthesize longer malto-oligosaccharides, production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Na+, K+, NH4-, and Li+ have essentially no effect on Pho1 activity, and no effect by 4 mM DTT
additional information
-
Na+, K+, NH4-, and Li+ have essentially no effect on Pho1 activity, and no effect by 4 mM DTT
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
Pho1 activity is strongly competitively inhibited by product phosphate in the synthesis reaction when amylopectin is the primer substrate, but this inhibition is less pronounced when short alpha-glucan chains are used as primers
additional information
-
no or poor inhibition by ribose 5-phosphate, glucose 6-phosphate, fructose-1,6-bisphosphate, ADP and UDP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glucose 1-phosphate
production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
phosphate
production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.69
phosphate
Pho1 with amylopectin as primer in the reaction, pH 6.5, 22°C
14.2
phosphate
Pho1 with short alpha-glucan chain as primer in the reaction, pH 6.5, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
seedlings of one and two weeks. When putting two weeks old seedlings under submerge conditions, enzyme activity rises steadily and reaches a maximum after 144 h and declines thereafter
loss of Pho1 causes smaller starch granules to accumulate and modifies the amylopectin structure. Pho1 plays a crucial role in starch biosynthesis in rice endosperm at low temperatures. One or more other factors can complement the function of Pho1 at high temperatures
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
plants contain two major Pho forms: the plastidial Pho1 or PhoL (low glycogen affinity) encoded by the PHO1 gene and a cytosolic Pho2 or PhoH (high glycogen affinity) encoded by the PHO2 gene
physiological function
the endosperm-specific plastidial alpha-glucan phosphorylase is important for synthesis of short-chain malto-oligosaccharides, it has an essential role during the initiation process of starch biosynthesis during rice seed development
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q9ATK9_ORYSA
928
0
104644
TrEMBL
other Location (Reliability: 4)
Q9FPE6_ORYSA
809
0
91491
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme in 50 mM imidazole, pH 7.0, 1 mM EDTA, 1 mM DTT, at 4°C, at least 2 weeks stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from seedlings, 299fold to homogeneity by protamine sulfate and ammonium sulfate fractionation, anion exchange chromatography, and dextrin affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hsu, J.H.; Yang, C.C.; Su, J.C.; Lee, P.D.
Purification and characterization of a cytosolic starch phosphorylase from etiolated rice seedlings
Bot. Bull. Acad. Sin.
45
187-196
2004
Oryza sativa
-
Das, A.; Pradhan, S.; Sharma, S.G.
Starch phosphorylase enzyme is over-expressed in submerged rice (Oryza sativa L) plant
J. Plant Biochem. Biotechnol.
15
51-53
2006
Oryza sativa
-
Satoh, H.; Shibahara, K.; Tokunaga, T.; Nishi, A.; Tasaki, M.; Hwang, S.K.; Okita, T.W.; Kaneko, N.; Fujita, N.; Yoshida, M.; Hosaka, Y.; Sato, A.; Utsumi, Y.; Ohdan, T.; Nakamura, Y.
Mutation of the plastidial alpha-glucan phosphorylase gene in rice affects the synthesis and structure of starch in the endosperm
Plant Cell
20
1833-1849
2008
Oryza sativa (B3IYE3), Oryza sativa
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