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Information on EC 2.4.1.11 - glycogen(starch) synthase

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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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UNIPROT: A8V967
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Word Map
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, tvag_258220, glycogen synthase-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
granule bound starch synthase
-
granule-bound starch synthase
-
starch synthase I
-
glucosyltransferase, uridine diphosphoglucose-glycogen
-
-
-
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glycogen synthetase (starch)
-
-
-
-
GSY2p
-
-
-
-
UDP-glucose-glycogen glucosyltransferase
-
-
-
-
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
-
-
-
-
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
ADP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n
ADP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
?
ADP-glucose + (1,4-alpha-D-glucosyl)n
ADP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
ADP-glucose + glycogen
ADP + ?
show the reaction diagram
-
-
-
?
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
the enzyme prefers UDP-alpha-D-glucose over ADP-alpha-D-glucose
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
UDP-glucose + amylopectin
UDP + amylose + ?
show the reaction diagram
enzyme polymerizes glucose residues to the outer chains of amylopectin. These chains subsequently are cleaved off amylopectin to generate mature amylose
-
-
?
UDP-glucose + glycogen
UDP + ?
show the reaction diagram
-
-
-
?
UDP-glucose + maltotriose
UDP + amylose
show the reaction diagram
-
-
-
?
additional information
?
-
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-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n
UDP + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
the enzyme prefers UDP-alpha-D-glucose over ADP-alpha-D-glucose
-
-
?
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
Cyanophora paradoxa synthesizes amylose with a granule-bound starch synthase displaying a preference for UDP-glucose
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
ADP-glucose
pH 7.5, 35°C
15
UDP-glucose
pH 7.5, 35°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A8V967_CYAPA
592
0
64140
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain bound to ADP and inhibitor acarbose, hanging drop vapor diffusion method, using 40 mM citric acid, 60 mM Bis-Tris propane, pH 6.4 and 20% (w/v) PEG 3350
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Tuner(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Plancke, C.; Colleoni, C.; Deschamps, P.; Dauvillee, D.; Nakamura, Y.; Haebel, S.; Ritte, G.; Steup, M.; Buleon, A.; Putaux, J.L.; Dupeyre, D.; dHulst, C.; Ral, J.P.; Loeffelhardt, W.; Ball, S.G.
Pathway of cytosolic starch synthesis in the model glaucophyte Cyanophora paradoxa
Eukaryot. Cell
7
247-257
2008
Cyanophora paradoxa (A8V967), Cyanophora paradoxa
Manually annotated by BRENDA team
Nielsen, M.M.; Ruzanski, C.; Krucewicz, K.; Striebeck, A.; Cenci, U.; Ball, S.G.; Palcic, M.M.; Cuesta-Seijo, J.A.
Crystal structures of the catalytic domain of Arabidopsis thaliana starch synthase IV, of granule bound starch synthase from CLg1 and of granule bound starch synthase I of Cyanophora paradoxa illustrate substrate recognition in starch synthases
Front. Plant Sci.
9
1138
2018
Cyanophora paradoxa (A8V967), Cyanophora paradoxa
Manually annotated by BRENDA team