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Information on EC 2.4.1.11 - glycogen(starch) synthase and Organism(s) Sus scrofa and UniProt Accession E0X6R4

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.11 glycogen(starch) synthase
IUBMB Comments
The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase).
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This record set is specific for:
Sus scrofa
UNIPROT: E0X6R4
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glycogen synthase, gbssi, granule-bound starch synthase, starch synthase i, granule bound starch synthase, gsy2p, glycogen synthase 2, gys-2, cg-gys, tvag_258220, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucosyltransferase, uridine diphosphoglucose-glycogen
-
-
-
-
glycogen synthetase (starch)
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-
-
-
GSY2p
-
-
-
-
UDP-glucose-glycogen glucosyltransferase
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-
-
-
UDP-glycogen synthase
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-
-
-
UDPG-glycogen synthetase
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-
-
-
UDPG-glycogen transglucosylase
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-
-
-
uridine diphosphoglucose-glycogen glucosyltransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:glycogen 4-alpha-D-glucosyltransferase
The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
9014-56-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
?
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
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
?
UDP-glucose + glycogen
glycogen + UDP
show the reaction diagram
-
-
-
-
?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycogen
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 0.508
UDP-glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.46
GYS2, sequence calculation
5.78
GYS1, sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GYS2; gene GYS2
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
subcutaneous, expression of GYS2
Manually annotated by BRENDA team
high expression level of GYS1
Manually annotated by BRENDA team
high expression level of GYS2
Manually annotated by BRENDA team
subcutaneous, GYS1
Manually annotated by BRENDA team
high expression level of GYS1
Manually annotated by BRENDA team
longissimus dorsi muscle, high expression level of GYS1
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
glycogen synthase catalyzes the key step of glycogen synthesis and plays an important role in glycogen metabolism in liver and muscle, phosphorylation sites regulate the activity of the enzyme
physiological function
glycogen synthase catalyzes the key step of glycogen synthesis and plays an important role in glycogen metabolism in liver and muscle, phosphorylation sites regulate the activity of the enzyme. Transcriptional regulation of GYS1 during myogenic differentiation in porcine satellite cells, overview. Effect of insulin is primarily mediated via posttranscriptional control the porcine glycogen synthase. Insulin promotes dephosphorylation of glycogen synthase in differentiated porcine satellite cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E0X6R4_PIG
702
0
80633
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80600
x * 80600, about, GYS2, sequence calculation
83700
x * 83700, about, GYS1, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 80600, about, GYS2, sequence calculation
?
x * 83700, about, GYS1, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
regulatory sites of GYS2 that undergo reversible phosphorylation are identified: two of them, sites 2 and 2a, are located near the N-terminus, while the remaining seven sites, 3a, 3b, 3c, 4, and 5 are found within the C-terminus, GYS2 does not contain sites 1a and 1b
phosphoprotein
regulatory sites of GYS1 that undergo reversible phosphorylation are identified: two of them, sites 2 and 2a, are located near the N-terminus, while the remaining seven sites, 3a, 3b, 3c, 4, 5, 1a, and 1b, are found within the C-terminus. Insulin promotes dephosphorylation of glycogen synthase in differentiated porcine satellite cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GYS2, in silico cloning, DNA and amino acid sequence determination and analysis, promoter determination and analysis, quantitative real-time RT-PCR tissue expression analysis
gene GYS1, in silico cloning, DNA and amino acid sequence determination and analysis, promoter determination and analysis, quantitative real-time RT-PCR tissue expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression level of GYS1 is upregulated from proliferation to differentiation in the porcine satellite cells
insulin does not significantly affect the transcription of GYS1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Passonneau, J.V.; Schwartz, J.P.; Rottenberg, D.A.
The partial purification and properties of pig brain glycogen synthase
J. Biol. Chem.
250
2287-2292
1975
Sus scrofa
Manually annotated by BRENDA team
Wang, L.; Xiong, Y.; Zuo, B.; Lei, M.; Ren, Z.; Xu, D.
Molecular and functional characterization of glycogen synthase in the porcine satellite cells under insulin treatment
Mol. Cell. Biochem.
360
169-180
2012
Sus scrofa (E0X6R2), Sus scrofa (E0X6R4), Sus scrofa, Sus scrofa Meishan (E0X6R2), Sus scrofa Meishan (E0X6R4)
Manually annotated by BRENDA team