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Information on EC 2.4.1.13 - sucrose synthase and Organism(s) Solanum tuberosum and UniProt Accession P10691
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2.4.1.13 sucrose synthaseIUBMB Comments
Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose [3-9]. Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP-glucose (necessary for starch biosynthesis) .
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Word Map
- 2.4.1.13
- invertase
- starch
- maize
-
sink
- cultivar
-
pyrophosphorylase
- grain
- endosperm
- crop
- seedling
- cellulose
- potato
- cotton
- tuber
- drought
- phloem
-
sucrose-phosphate
- fructokinase
- kernel
- hexoses
- hexokinase
- agpase
-
3.2.1.26
-
anthesis
- callose
- hirsutum
- sugarcane
-
photosynthate
- panicle
- fructans
-
granule-bound
-
gossypium
-
grain-filling
-
photoassimilate
- adpglucose
- spikelet
-
source-sink
-
boll
- saccharum
- synthesis
- stachyose
-
amyloplasts
- taproot
- agriculture
The taxonomic range for the selected organisms is: Solanum tuberosum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sucrose synthase, sucrose synthetase, susy1, mtsucs1, rsus3, sucrose synthase 1, psnsusy2, susy2, sucrose synthase 2, sucrose synthase 3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosyltransferase, uridine diphosphoglucose-fructose
-
-
-
-
sucrose synthetase
-
-
-
-
sucrose-UDP glucosyltransferase
-
-
-
-
sucrose-uridine diphosphate glucosyltransferase
-
-
-
-
Sus
sus4
SuSy
UDP-glucose-fructose glucosyltransferase
-
-
-
-
UDP-glucose:D-fructose 2-alpha-D-glucosyltransferase
-
-
-
-
uridine diphosphoglucose-fructose glucosyltransferase
-
-
-
-
Sus
-
-
-
-
SuSy
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
NDP-glucose:D-fructose 2-alpha-D-glucosyltransferase
Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose [3-9]. Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP-glucose (necessary for starch biosynthesis) [10].
CAS REGISTRY NUMBER
COMMENTARY
9030-05-1
-
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
UDP-alpha-D-glucose + 1-deoxy-1-fluoro-fructose
?
the recombinant enzyme expressed in Escherichia coli shows 175% of the activity with D-fructose, 100% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + D-glucose
?
the recombinant enzyme expressed in Sacchromyces cerevisiae shows 2% of the activity with D-fructose, no activity with the enzyme expressed in Escherichia coli
-
-
?
UDP-alpha-D-glucose + D-lyxose
?
the recombinant enzyme expressed in Escherichia coli shows 150% of the activity with D-fructose, 48% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + D-mannose
?
the recombinant enzyme expressed in Escherichia coli shows 75% of the activity with D-fructose, 40% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + D-ribose
?
the recombinant enzyme expressed in Sacchromyces cerevisiae shows 7% of the activity with D-fructose, no activity with the enzyme expressed in Escherichia coli
-
-
?
UDP-alpha-D-glucose + D-ribulose
?
the recombinant enzyme expressed in Escherichia coli shows 24% of the activity with D-fructose, no activity with enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + D-tagatose
?
the recombinant enzyme expressed in Escherichia coli shows 43% of the activity with D-fructose, no activity with the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + D-talose
?
the recombinant enzyme expressed in Sacchromyces cerevisiae shows 117% of the activity with D-fructose, no activity with the enzyme expressed in Escherichia coli
-
-
?
UDP-alpha-D-glucose + L-arabinose
?
the recombinant enzyme expressed in Escherichia coli shows 490% of the activity with D-fructose, 36% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + L-galactose
?
the recombinant enzyme expressed in Sacchromyces cerevisiae shows 2% of the activity with D-fructose, no activity with the enzyme expressed in Escherichia coli
-
-
?
UDP-alpha-D-glucose + L-glucose
?
the recombinant enzyme expressed in Escherichia coli shows 34% of the activity with D-fructose, no activity with the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + L-mannose
?
the recombinant enzyme expressed in Escherichia coli shows 59% of the activity with D-fructose, 8% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + L-rhamnose
?
the recombinant enzyme expressed in Escherichia coli shows 52% of the activity with D-fructose, no activity with the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + L-sorbose
?
the recombinant enzyme expressed in Escherichia coli shows 96% of the activity with D-fructose, 55% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
NDP + sucrose
NDP-alpha-D-glucose + D-fructose
-
the reaction is catalyzed at low pH values
-
-
r
NDP-alpha-D-glucose + D-fructose
NDP + sucrose
-
the reaction is catalyzed at high pH values
-
-
r
UDP-alpha-D-galactose + D-fructose
UDP + sucrose
-
23% of the activity with UDP-alpha-D-glucose
-
-
?
UDP-alpha-D-glucuronic acid + D-fructose
?
-
32% of the activity with UDP-alpha-D-glucose
-
-
?
UDP-alpha-D-xylose + D-fructose
?
-
39% of the activity with UDP-alpha-D-glucose
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + D-fructose
UDP + beta-D-fructofuranosyl 2-(acetylamino)-2-deoxy-alpha-D-galactopyranoside
-
23% of the activity with UDP-alpha-D-glucose
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + D-fructose
UDP + 2-acetamido-2-deoxy-D-glucopyranosyl-beta-D-fructofuranoside
additional information
?
-
substrate specificities of recombinant wild-type and mutant enzymes expressed in Escherichia coli or in Saccharomyces cerevisia, overview
-
-
?
UDP-alpha-D-glucose + D-xylose
?
the recombinant enzyme expressed in Escherichia coli shows 300% of the activity with D-fructose, 14% for the enzyme expressed in Sacchromyces cerevisiae
-
-
?
UDP-alpha-D-glucose + D-xylose
?
the recombinant enzyme expressed in Sacchromyces cerevisiae shows 42% of the activity with D-fructose, no activity with the enzyme expressed in Escherichia coli
-
-
?
ADP + sucrose
ADP-glucose + D-fructose
-
sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants
-
-
r
ADP + sucrose
ADP-glucose + D-fructose
ADP-glucose produced by SuSy is linked to starch biosynthesis. SuSy exerts a strong control on the starch biosynthetic process and controls the production of ADP-glucose accumulating in source leaves
-
-
?
UDP + sucrose
UDP-glucose + D-fructose
-
biochemical pathway for sucrose degradation. Repression of invertase and mobilization of sucrose via the energetically less costly route provided by SuSY is important in growing tubers because it conserves oxygen and allows higher internal oxygen tensions to be maintained
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + D-fructose
UDP + 2-acetamido-2-deoxy-D-glucopyranosyl-beta-D-fructofuranoside
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + D-fructose
UDP + 2-acetamido-2-deoxy-D-glucopyranosyl-beta-D-fructofuranoside
-
as active as UDP-alpha-D-glucose
-
-
?
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
NDP + sucrose
NDP-alpha-D-glucose + D-fructose
-
the reaction is catalyzed at low pH values
-
-
r
NDP-alpha-D-glucose + D-fructose
NDP + sucrose
-
the reaction is catalyzed at high pH values
-
-
r
UDP + sucrose
UDP-glucose + D-fructose
-
biochemical pathway for sucrose degradation. Repression of invertase and mobilization of sucrose via the energetically less costly route provided by SuSY is important in growing tubers because it conserves oxygen and allows higher internal oxygen tensions to be maintained
-
-
?
ADP + sucrose
ADP-glucose + D-fructose
-
sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants
-
-
r
ADP + sucrose
ADP-glucose + D-fructose
ADP-glucose produced by SuSy is linked to starch biosynthesis. SuSy exerts a strong control on the starch biosynthetic process and controls the production of ADP-glucose accumulating in source leaves
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
D-fructose
recombinant enzyme expressed in Saccharomyces cerevisiae
0.6
UDP-alpha-D-glucose
recombinant enzyme expressed in Saccharomyces cerevisiae
1.4
UDP-alpha-D-glucose
recombinant enzyme expressed in Escherichia coli
1.4
D-fructose
-
with UDP-alpha-D-glucose as cosubstrate, at pH 7.5 and 37°C
5.5
D-fructose
-
isoform SUS1, with UDP-alpha-D-glucose as cosubstrate, at pH 9.0 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
D-fructose
-
isoform SUS1, with UDP-alpha-D-glucose as cosubstrate, at pH 9.0 and 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
purified recombinant enzyme, expressed in Saccharomyces cerevisiae
additional information
-
SuSy activity: 90 mU/g FW in wild-type tubers, 170-250 mU/g FW in transgenic overexpressing tubers
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is important in starcj biosynthesis in potato tubers, changes in SuSy activity do not affect the expression of genes directly involved in starch metabolism, but might lead to important changes in the tuber metabolome and N -glycome
physiological function
physiological function
sucrose synthase is a major determinant of sink strength that highly controls the channeling of incoming sucrose into starch and cell wall polysaccharides, the enzyme is involved in production of starch and ADP-glucose
physiological function
-
guard cell-specific isoform SUS3 overexpression leads to increased enzyme activity, stomatal aperture, stomatal conductance, transpiration rate, net photosynthetic rate and growth
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). SUS1_SOLTU
805
0
92416
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S11A
site-directed mutagenesis, the mutant enzyme shows an altered monosacchride accceptor substrate specificity compared to the wild-type enzyme when expressed in Saccharomyces cerevisiae
S11D
site-directed mutagenesis, the mutant enzyme shows an altered monosacchride accceptor substrate specificity compared to the wild-type enzyme when expressed in Escherichia coli
additional information
-
construction of transgenic enzyme overexpressing plants and of transgenic antisense plants. ADPG diphosphorylase and UDPG diphosphorylase activities in tubers from overexpressing plants are significantly higher than in control tubers, whereas ADPG diphosphorylase activities in tubers of one SuSy line are significantly lower than in control tubers
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes 450fold from Escherichia coli and 25fold from Saccharomyces cerevisiae by ion exchange and immobilized metal affinity chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sus1, expression of wild-type enzyme and mutant S11D in Escherichia coli strain BL21(DE3) reveals monosaccharides D-ribulose, D-tagatose, L-glucose, and L-rhamnose as additional acceptor substrates, expression of wild-type SuSy1 and SuSy1 S11A mutant in Saccharomyces cerevisiae strain BY4741 with phosphorylation of the wild-type enzyme at Ser11
DNA and amino acid sequence determination and analysis, phylogenetic analysis
expressed in Escherichia coli BL21(DE3) and Saccharomyces. cerevisiae 22574d cells
-
gene SUS4, recombinant ectopic expression of the enzyme in Zea mays seed endosperm. Transgenic developing seeds exhibit a significant increase in SuSy activity, the transgenic seeds accumulate 10-15% more starch at the mature stage and contain a higher amylose/amylopectin balance than wild-type maize seeds, while no significant changes are detected in the transgenic seeds in the content of soluble sugars, and in activities of starch metabolism-related enzymes when compared with wild-type seeds, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murata, T.
Sucrose synthetase of rice grains and potato tubers
Agric. Biol. Chem.
36
1815-1818
1972
Oryza sativa, Solanum tuberosum
-
Roemer, U.; Rupprath, C.; Elling, L.
The donor substrate spectrum of recombinant sucrose synthase 1 from potato for the synthesis of sucrose analogs
Adv. Synth. Catal.
345
684-686
2003
Solanum tuberosum
-
Rmer, U.; Schrader, H.; Gunther, N.; Nettelstroth, N.; Frommer, W.B.; Elling, L.
Expression, purification and characterization of recombinant sucrose synthase 1 from Solanum tuberosum L. for carbohydrate engineering
J. Biotechnol.
107
135-149
2004
Solanum tuberosum
Baroja-Fernandez, E.; Munoz, F.J.; Saikusa, T.; Rodriguez-Lopez, M.; Akazawa, T.; Pozueta-Romero, J.
Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants
Plant Cell Physiol.
44
500-509
2003
Hordeum vulgare, Solanum tuberosum
Bologa, K.L.; Fernie, A.R.; Leisse, A.; Loureiro, M.E.; Geigenberger, P.
A bypass of sucrose synthase leads to low internal oxygen and impaired metabolic performance in growing potato tubers
Plant Physiol.
132
2058-2072
2003
Solanum tuberosum
Munoz, F.J.; Baroja-Fernandez, E.; Moran-Zorzano, M.T.; Viale, A.M.; Etxeberria, E.; Alonso-Casajus, N.; Pozueta-Romero, J.
Sucrose synthase controls both intracellular ADP glucose levels and transitory starch biosynthesis in source leaves
Plant Cell Physiol.
46
1366-1376
2005
Solanum tuberosum (Q7Y078), Solanum tuberosum
Sauerzapfe, B.; Engels, L.; Elling, L.
Broadening the biocatalytic properties of recombinant sucrose synthase 1 from potato (Solanum tuberosum L.) by expression in Escherichia coli and Saccharomyces cerevisiae
Enzyme Microb. Technol.
43
289-296
2008
Solanum tuberosum (P10691)
-
Abid, G.; Silue, S.; Muhovski, Y.; Jacquemin, J.M.; Toussaint, A.; Baudoin, J.P.
Role of myo-inositol phosphate synthase and sucrose synthase genes in plant seed development
Gene
439
1-10
2009
Arabidopsis thaliana (F4K5W8), Arabidopsis thaliana (P49040), Arabidopsis thaliana (Q00917), Citrus unshiu (Q9SLY2), Citrus x paradisi, Coffea arabica (Q0E7D4), Daucus carota (O49845), Eucalyptus grandis (Q00P15), Eucalyptus grandis (Q00P16), Glycine max (P13708), Glycine max, Gossypium hirsutum (Q9XGB7), Gossypium hirsutum, Oryza sativa (P31924), Pisum sativum (O24301), Pisum sativum (O81610), Pisum sativum (Q9AVR8), Pisum sativum (Q9T0M9), Solanum lycopersicum (P49037), Solanum tuberosum (Q84T18), Vicia faba (P31926), Zea mays
Baroja-Fernandez, E.; Munoz, F.J.; Montero, M.; Etxeberria, E.; Sesma, M.T.; Ovecka, M.; Bahaji, A.; Ezquer, I.; Li, J.; Prat, S.; Pozueta-Romero, J.
Enhancing sucrose synthase activity in transgenic potato (Solanum tuberosum L.) tubers results in increased levels of starch, ADPglucose and UDPglucose and total yield
Plant Cell Physiol.
50
1651-1662
2009
Solanum tuberosum
Li, J.; Baroja-Fernandez, E.; Bahaji, A.; Munoz, F.J.; Ovecka, M.; Montero, M.; Sesma, M.T.; Alonso-Casajus, N.; Almagro, G.; Sanchez-Lopez, A.M.; Hidalgo, M.; Zamarbide, M.; Pozueta-Romero, J.
Enhancing sucrose synthase activity results in increased levels of starch and ADP-glucose in maize (Zea mays L.) seed endosperms
Plant Cell Physiol.
54
282-294
2013
Zea mays, Solanum tuberosum (Q7Y078), Solanum tuberosum
Schmoelzer, K.; Gutmann, A.; Diricks, M.; Desmet, T.; Nidetzky, B.
Sucrose synthase A unique glycosyltransferase for biocatalytic glycosylation process development
Biotechnol. Adv.
34
88-111
2016
Anabaena sp., Arabidopsis thaliana, Beta vulgaris, Vicia faba, Helianthus tuberosus, Hordeum vulgare, Ipomoea batatas, Manihot esculenta, Nitrosomonas europaea, Oryza sativa, Vigna radiata, Pisum sativum, Prunus persica, Pyrus pyrifolia, Saccharum sp., Solanum tuberosum, Zea mays, Thermosynechococcus vestitus, Acidithiobacillus caldus, Solanum chmielewskii, Glycine max (P13708)
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