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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Triticum aestivum and UniProt Accession Q9LKJ3
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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: Triticum aestivum
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 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
glycogen + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
-
-
-
r
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
the cytosolic isozyme
-
-
r
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
the cytosolic isozyme
-
-
r
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
the cytosolic isozyme
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
the cytosolic isozyme is involved in the processing of incoming carbohydrate during rapid tissue growth, plastidic isozyme is associated with transitory leaf starch metabolism and with the initiation of seed endosperm reserve starch accumulation, but it plays no role in the degradation of the reserve starch
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
the cytosolic isozyme utilizes amylopectin, amylose, soluble starch, and glycogen as polysaccharide substrates, while the plastidic isozyme prefers starch
-
-
r
additional information
?
-
substrate specificity of cytosolic isozyme
-
-
?
additional information
?
-
-
substrate specificity of cytosolic isozyme
-
-
?
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
the cytosolic isozyme is involved in the processing of incoming carbohydrate during rapid tissue growth, plastidic isozyme is associated with transitory leaf starch metabolism and with the initiation of seed endosperm reserve starch accumulation, but it plays no role in the degradation of the reserve starch
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44
maltotetraose
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
0.03
amylopectin
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
0.03
amylopectin
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
0.81
maltoheptaose
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
4.49
maltoheptaose
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
0.1
soluble starch
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
-
0.15
soluble starch
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytosolic isozyme; var. Star, 3 tissue-dependent enzyme isoforms P1, P2, and P3
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
young and mature, the latter contain only the plastidic isozyme
germinated seeds contain only the cytosolic isozyme restricted to the embryo
Pho activity is observed in highly purified amyloplast extracts prepared from developing wheat endosperms. Protein and enzyme activity increase throughout the period of starch synthesis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoform Pho1 may play an important role in recycling glucosyl units from malto-oligosaccharides back into starch synthesis in the developing wheat endosperm. Protein and enzyme activity increase throughout the period of starch synthesis
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). PHSH_WHEAT
832
0
93612
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic isozyme from leaves 7140fold to homogeneity by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schupp, N.; Ziegler, P.
The relation of starch phosphorylases to starch metabolism in wheat
Plant Cell Physiol.
45
1471-1484
2004
Triticum aestivum (Q9LKJ3), Triticum aestivum
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