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Information on EC 2.4.1.21 - starch synthase (glycosyl-transferring) and Organism(s) Escherichia coli and UniProt Accession P0A6U8

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.21 starch synthase (glycosyl-transferring)
IUBMB Comments
The accepted name varies according to the source of the enzyme and the nature of its synthetic product, e.g. starch synthase, bacterial glycogen synthase. Similar to EC 2.4.1.11 [glycogen(starch) synthase] but the preferred or mandatory nucleoside diphosphate sugar substrate is ADP-alpha-D-glucose. The entry covers starch and glycogen synthases utilizing ADP-alpha-D-glucose.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A6U8
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
starch synthase, ssiia, gsase, ssiii, granule-bound starch synthase i, ssiiia, starch synthase iia, starch synthetase, starch synthase iii, starch synthase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycogen synthase
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adenosine diphosphate glucose-starch glucosyltransferase
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-
-
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adenosine diphosphoglucose-starch glucosyltransferase
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-
-
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ADP-glucose starch synthase
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-
-
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ADP-glucose synthase
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-
-
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ADP-glucose transglucosylase
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-
-
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ADP-glucose-starch glucosyltransferase
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-
-
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ADPG starch synthetase
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-
-
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ADPG-starch glucosyltransferase
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-
-
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glucosyltransferase, adenosine diphosphoglucose-starch
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-
-
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starch synthetase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ADP-glucose:(1->4)-alpha-D-glucan 4-alpha-D-glucosyltransferase
The accepted name varies according to the source of the enzyme and the nature of its synthetic product, e.g. starch synthase, bacterial glycogen synthase. Similar to EC 2.4.1.11 [glycogen(starch) synthase] but the preferred or mandatory nucleoside diphosphate sugar substrate is ADP-alpha-D-glucose. The entry covers starch and glycogen synthases utilizing ADP-alpha-D-glucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-10-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-glucose + alpha-1,4-polyglucan
ADP + alpha-1,4-polyglucan
show the reaction diagram
UDP-glucose + (1,4-alpha-D-glucosyl)n
UDP + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucono-1,5-lactone
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inhibition of glycogen synthase I and II
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-alpha-Glucan branching enzyme
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EC 2.4.1.18, stimulation of unprimed reaction
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ammonium sulfate
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beta-Lactoglobulin
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activation of unprimed reaction
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Bovine plasma albumin
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activation of unprimed reaction
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hemoglobin
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activation of unprimed reaction
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myoglobin
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activation of unprimed reaction
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NaF
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500 mM, strong activation of unprimed reaction
ovomucoid
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activation of unprimed reaction
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potassium acetate
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500 mM, strong activation of unprimed reaction
Sodium acetate
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500 mM, strong activation of unprimed reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
ADPglucose
2.7
UDPglucose
-
-
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
D-glucono-1,5-lactone
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
494
-
glycogen synthase I
505
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glcogen synthase II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
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2 * 49000, SDS-PAGE
92700
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sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 49000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization of the inactive glycogen synthase mutant E377A with substrate ADPGlc and cocrystallization of wild-type glycogen synthase with substrate ADPGlc and the glucan acceptor mimic 4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid, i.e. HEPPSO produces a closed form of glycogen synthase and suggests that domain-domain closure accompanies glycogen synthesis. Four bound oligosaccharides are observed, G6a in the interdomain cleft and G6b, G6c, and G6d on the N-terminal domain surface. Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of glycogen synthase. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement
structure of the wild-type enzyme bound to ADP and glucose reveals a 15.2° overall domain-domain closure. The main chain carbonyl group of His-161, Arg-300, and Lys-305 are suggested to act as critical catalytic residues in the transglycosylation. Glu-377 is found on the-face of the glucose and plays an electrostatic role in the active site and as a glucose ring locator. In the mutant E377A-ADP-4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid complex the glucose moiety is either absent or disordered in the active site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C7S/C409S
exhibits comparable specific activity and apparent affinity for ADP-Glc to wild-type. Use as alternative in crystallization trials to avoid aggregation
E377A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-85°C, at least 1 year
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 isozymes, DEAE-cellulose, 4-aminobutyl-Sepharose, Bio-Gel P200
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Holmes, E.; Preiss, J.
Characterization of Escherichia coli B glycogen synthase enzymatic reactions and products
Arch. Biochem. Biophys.
196
436-448
1979
Escherichia coli
Manually annotated by BRENDA team
Fox, J.; Kawaguchi, K.; Greenberg, E.; Preiss, J.
Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B ADPglucose:1,4-alpha-D-glucan 4-alpha-glucosyltransferase
Biochemistry
15
849-856
1976
Escherichia coli
Manually annotated by BRENDA team
Fox, J.; Kennedy, L.D.; Hawker, J.S.; Ozbun, J.L.; Greenberg, E.; Lammel, C.; Preiss, J.
De novo synthesis of bacterial glycogen and plant starch by ADPG: alpha-glucan 4-glucosyl transferase
Ann. N. Y. Acad. Sci.
210
90-103
1973
Escherichia coli, Spinacia oleracea
Manually annotated by BRENDA team
Imparl-Radosevich, J.M.; Li, P.; Zhang, L.; McKean, A.L.; Keeling, P.L.; Guan, H.
Purification and characterization of maize starch synthase I and its truncated forms
Arch. Biochem. Biophys.
353
64-72
1998
Escherichia coli, Zea mays
Manually annotated by BRENDA team
Sheng, F.; Yep, A.; Feng, L.; Preiss, J.; Geiger, J.H.
Oligosaccharide binding in Escherichia coli glycogen synthase
Biochemistry
48
10089-10097
2009
Escherichia coli (P0A6U8), Escherichia coli
Manually annotated by BRENDA team
Sheng, F.; Jia, X.; Yep, A.; Preiss, J.; Geiger, J.H.
The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase
J. Biol. Chem.
284
17796-17807
2009
Escherichia coli (P0A6U8), Escherichia coli
Manually annotated by BRENDA team