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Enzyme Nomenclature
Information on EC 2.4.1.13 - sucrose synthase
Word Map on EC 2.4.1.13
- 2.4.1.13
- invertase
- starch
- maize
-
sink
- hexose
-
pyrophosphorylase
- leaf
- endosperm
-
photosynthetic
- potato
- cultivar
- tuber
- phloem
- kernel
-
pollination
-
3.2.1.26
-
sucrose-phosphate
- callose
- fructokinase
-
anthesis
-
granule-bound
- adpglucose
- saccharum
-
fructans
-
amyloplasts
- sugarcane
-
photoassimilate
- hirsutum
-
photosynthate
-
source-sink
- stachyose
-
pyrophosphate-dependent
-
leghemoglobins
- adp-glc
- agriculture
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.4.1.13
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RECOMMENDED NAME
GeneOntology No.
sucrose synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NDP-glucose + D-fructose = NDP + sucrose
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9030-05-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 genotypes ICPL 84023 and ICP 301 tolerant to waterlogging stress, and 2 genotypes ICP 7035 and Pusa 207 susceptible to waterlogging stress
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syncytia induced by nematode Heterodera schachtii
UniProt
Sona, a small-seeded desi cultivar, and Kaniva, a large-seeded kabuli cultivar
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two cultivars, cv. Shanyou 63 and Liangyoupeijiu, Peiai 64S/93-11, an indica/indica F1 hybrid
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cultivar BY535 with a high starch content and culitvar JM20 with a low starch content
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Populus alba overexpressing a S11E mutant form of Vigna radiata SuSy, the mutation causes a decrease in Km-value for sucrose by a factor of 7
Uniprot
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Nitrosomonas europaea sucrose synthase shares the same fold as the GT-B family of the retaining glycosyltransferases
evolution
the enzyme belongs to family 4 of the glycosyltransferases (GT4) and contains an E-X7-E motif that is conserved in members of GT4 and two other GT families, sequence comparisons, overview
malfunction
systemically affected sugar levels and enzyme activities in the shoots of the enzyme mutants, suggesting changes in the source-sink relationship. In sink tissues, sucrose is cleaved to make glucose and fructose available for energy-gaining reactions, macromolecule and amino acid biosynthesis. Heterodera schachtii root infection affects systemic sucrose processing; systemically affected sugar levels and enzyme activities in the shoots of the enzyme mutants, suggesting changes in the source-sink relationship. In sink tissues, sucrose is cleaved to make glucose and fructose available for energy-gaining reactions, macromolecule and amino acid biosynthesis. Heterodera schachtii root infection affects systemic sucrose processing; systemically affected sugar levels and enzyme activities in the shoots of the enzyme mutants, suggesting changes in the source-sink relationship. In sink tissues, sucrose is cleaved to make glucose and fructose available for energy-gaining reactions, macromolecule and amino acid biosynthesis. Heterodera schachtii root infection affects systemic sucrose processing; systemically affected sugar levels and enzyme activities in the shoots of the enzyme mutants, suggesting changes in the source-sink relationship. In sink tissues, sucrose is cleaved to make glucose and fructose available for energy-gaining reactions, macromolecule and amino acid biosynthesis. Heterodera schachtii root infection affects systemic sucrose processing; systemically affected sugar levels and enzyme activities in the shoots of the enzyme mutants, suggesting changes in the source-sink relationship. In sink tissues, sucrose is cleaved to make glucose and fructose available for energy-gaining reactions, macromolecule and amino acid biosynthesis. Heterodera schachtii root infection affects systemic sucrose processing; systemically affected sugar levels and enzyme activities in the shoots of the enzyme mutants, suggesting changes in the source-sink relationship. In sink tissues, sucrose is cleaved to make glucose and fructose available for energy-gaining reactions, macromolecule and amino acid biosynthesis. Heterodera schachtii root infection affects systemic sucrose processing
malfunction
mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance, lower tolerance of the sus1/sus4 mutant for hypoxia compared to wild-type; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance, lower tolerance of the sus1/sus4 mutant for hypoxia compared to wild-type
malfunction
antisense suppression of Cucumis sativus sucrose synthase 3 reduces hypoxic stress tolerance
malfunction
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mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance, lower tolerance of the sus1/sus4 mutant for hypoxia compared to wild-type; mutants defective in sucrose synthase display a conditional phenotype in terms of low-oxygen tolerance, lower tolerance of the sus1/sus4 mutant for hypoxia compared to wild-type
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malfunction
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antisense suppression of Cucumis sativus sucrose synthase 3 reduces hypoxic stress tolerance
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metabolism
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significant and positive association between seed and pod wall dry weight at maturity and peak sucrose synthase activity in seeds of both cultivars and both treatments, irrigation and under a rainout shelter, used to induce terminal drought
metabolism
sucrose synthase is involved in UDP-glucose formation, the principal nucleoside diphosphate in the sucrose cleavage reaction and in trehalose biosynthesis; sucrose synthase is involved in UDP-glucose formation, the principal nucleoside diphosphate in the sucrose cleavage reaction and in trehalose biosynthesis; sucrose synthase is involved in UDP-glucose formation, the principal nucleoside diphosphate in the sucrose cleavage reaction and in trehalose biosynthesis
metabolism
sucrose synthase is involved in UDP-glucose formation, the principal nucleoside diphosphate in the sucrose cleavage reaction and in trehalose biosynthesis
metabolism
sucrose synthase is involved in UDP-glucose formation, the principal nucleoside diphosphate in the sucrose cleavage reaction and in trehalose biosynthesis; sucrose synthase is involved in UDP-glucose formation, the principal nucleoside diphosphate in the sucrose cleavage reaction and in trehalose biosynthesis
metabolism
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sucrose synthase is a key enzyme regulating the process of rice grain filling meaning conversion of sucrose into starch
metabolism
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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
metabolism
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sucrose synthase is an integral component of the cellulose synthesis
metabolism
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interaction between sucrose and glycogen metabolism
metabolism
the enzyme is involved in the metabolic regulation of the sucrose metabolism, overview; the enzyme is involved in the metabolic regulation of the sucrose metabolism, overview; the enzyme is involved in the metabolic regulation of the sucrose metabolism, overview; the enzyme is involved in the metabolic regulation of the sucrose metabolism, overview; the enzyme is involved in the metabolic regulation of the sucrose metabolism, overview; the enzyme is involved in the metabolic regulation of the sucrose metabolism, overview
physiological function
the enzyme is involved in various physiological processes including seed growth and resistance to biotic and abiotic stresses; the enzyme is involved in various physiological processes including seed growth and resistance to biotic and abiotic stresses; the enzyme is involved in various physiological processes including seed growth and resistance to biotic and abiotic stresses
physiological function
the enzyme is involved in various physiological processes including seed growth and resistance to biotic and abiotic stresses
physiological function
the enzyme is involved in various physiological processes including seed growth and resistance to biotic and abiotic stresses; the enzyme is involved in various physiological processes including seed growth and resistance to biotic and abiotic stresses
physiological function
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sucrose synthase is the main sucrose breakdown enzyme in plant sink tissues. Sucrose synthase levels do not limit or regulate carbon transfer in the arbuscular mycorrhizal symbiosis
physiological function
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the enzyme may play little role in determining sucrose accumulation during muskmelon fruit
physiological function
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the symbiosis-induced Medicago truncatula sucrose synthase gene MtSucS1 is required for an efficient arbuscular mycorrhiza, overview
physiological function
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SuSy activation is associated with the rapid accumulation of sucrose in peach fruit. In sink organs, SuSy displays typically the predominant sucrolytic activity
physiological function
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in sugar-starved cells, the in situ activity of both sucrose synthase and invertase decrease significantly. Following supplementation of root meristems with sugar, invertase remaines inactive, but sucrose synthase activity increases. In sugar-starved cells, sucrose synthase activity is induced more by exogenous sucrose than by glucose. The sucrose-induced activity is strongly inhibited by okadaic acid and less by 6-dimethylaminopurine at early stages of regeneration, but not at the stages preceding DNA replication or mitotic activities. Prolongation of regeneration and a marked decrease in the number of cells resuming proliferation and resulting from the action of inhibitors, are correlated with the process of sucrose synthase activation at the beginning of regeneration from sugar starvation
physiological function
sucrose synthase activity is negatively correlated with sucrose and positively correlated with hexose sugars
physiological function
cell wall-localized isoform SusC may provide UDP-glucose for cellulose and callose synthesis from extracellular sugars
physiological function
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enzymic activities in organs of a mutant lacking the activities of isoforms sus1, sus2, sus3, sus4 is about 80-90% of those found in wild-type
physiological function
isoform Sus2 knockout mutant shows 30-50% less sucrose synthase activity than wild-type and therefore accumulates 40% more sucrose and 50% less fructose at 15 days after flowering. Mutation does not affect the hexose phosphate pool, but leads to 30-70% less starch in embryo and seed coat. Lipid content is are 55% higher at 9-15 days after flowering. Final seed size and composition are unaltered due to an earlier cessation of growth, thus giving rise to an apparent silent phenotype of mature mutant seeds; isoform Sus3 knockout mutant shows 30-50% less sucrose synthase activity than wild-type and therefore accumulates 40% more sucrose and 50% less fructose at 15 days after flowering. Mutation does not affect the hexose phosphate pool, but leads to 30-70% less starch in embryo and seed coat. Lipid content is are 55% higher at 9-15 days after flowering. Final seed size and composition are unaltered due to an earlier cessation of growth, thus giving rise to an apparent silent phenotype of mature mutant seeds
physiological function
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mutant lacking isoforms sus1/sus2/sus3/sus4 displays wild-type SUS5 and SUS6 expression levels in leaf, whereas leaves of the sus5/sus6 mutant display wild-type SUS1-4 expression levels. Sucrose synthase activity in leaves and stems of the sus1/sus2/sus3/sus4 and sus5/sus6 plants is about 85% of that of wild-type leaves, which can support normal cellulose and starch biosynthesis; mutant lacking isoforms sus1/sus2/sus3/sus4 displays wild-type SUS5 and SUS6 expression levels in leaf, whereas leaves of the sus5/sus6 mutant display wild-type SUS1-4 expression levels. Sucrose synthase activity in leaves and stems of the sus1/sus2/sus3/sus4 and sus5/sus6 plants is about 85% of that of wild-type leaves, which can support normal cellulose and starch biosynthesis
physiological function
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in filamentous cyanobacteria, the sucrose cleavage direction plays a key physiological function in carbon metabolism, nitrogen fixation, and stress tolerance
physiological function
role of the sucrose-cleaving enzymes sucrose synthases in the development of endoparasitic nematodes, the cyst forming Heterodera schachtii and the root-knot forming Meloidogyne javanica. The parasites influence the regulation of enzyme transcription, general role of sucrose-degrading enzymes during plant-nematode interactions, overview. Sucrose synthases play particular roles in nematode-induced feeding sites; role of the sucrose-cleaving enzymes sucrose synthases in the development of endoparasitic nematodes, the cyst forming Heterodera schachtii and the root-knot forming Meloidogyne javanica. The parasites influence the regulation of enzyme transcription, general role of sucrose-degrading enzymes during plant-nematode interactions, overview. Sucrose synthases play particular roles in nematode-induced feeding sites; role of the sucrose-cleaving enzymes sucrose synthases in the development of endoparasitic nematodes, the cyst forming Heterodera schachtii and the root-knot forming Meloidogyne javanica. The parasites influence the regulation of enzyme transcription, general role of sucrose-degrading enzymes during plant-nematode interactions, overview. Sucrose synthases play particular roles in nematode-induced feeding sites; role of the sucrose-cleaving enzymes sucrose synthases in the development of endoparasitic nematodes, the cyst forming Heterodera schachtii and the root-knot forming Meloidogyne javanica. The parasites influence the regulation of enzyme transcription, general role of sucrose-degrading enzymes during plant-nematode interactions, overview. Sucrose synthases play particular roles in nematode-induced feeding sites; role of the sucrose-cleaving enzymes sucrose synthases in the development of endoparasitic nematodes, the cyst forming Heterodera schachtii and the root-knot forming Meloidogyne javanica. The parasites influence the regulation of enzyme transcription, general role of sucrose-degrading enzymes during plant-nematode interactions, overview. Sucrose synthases play particular roles in nematode-induced feeding sites; role of the sucrose-cleaving enzymes sucrose synthases in the development of endoparasitic nematodes, the cyst forming Heterodera schachtii and the root-knot forming Meloidogyne javanica. The parasites influence the regulation of enzyme transcription, general role of sucrose-degrading enzymes during plant-nematode interactions, overview. Sucrose synthases play particular roles in nematode-induced feeding sites
physiological function
role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Isozyme SUS1 is not required for the sucrose-ethanol transition in seedlings under low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Isozyme SUS4 is not required for the sucrose-ethanol transition in seedlings under low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia
physiological function
CsSUS3 participates in resisting hypoxic stress, mechanism analysis
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
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enhancing sucrose synthase activity results in increased levels of starch and ADP-glucose in maize seed endosperms
physiological function
the enzyme activity is finely tuned through regulation of their gene expression at different levels and modulation of enzymatic activities by metabolites
physiological function
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sucrose synthase is considered the first key enzyme for secondary growth because it is a highly regulated cytosolic enzyme that catalyzes the reversible conversion of sucrose and UDP into UDP-glucose and fructose. Enzyme PsnSuSy2 plays a significant role in cleaving sucrose into UDP-glucose and fructose to facilitate cellulose biosynthesis and that promotion of cellulose biosynthesis suppresses lignin biosynthesis
physiological function
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low enzyme activity during cambial growth reduces sink capacity of xylem tissues, thus leading to a considerable increase in the sucrose content in the phloem, which can alter the program of cell development in the cambial zone of Karelian birch. Specific texture of Karelian birch wood emerges as a result of deviations in cambial activity, overview. Upon the decline in cambial activity, the dynamics of changes in enzyme activity in Karelian birch is similar to that in common birch: in xylem tissues the enzyme activity becomes lower but the lowering is not as strong as in Betula pendula var. pendula. In phloem tissues the enzyme activity increases but, in contrast to common birch, this increase is not accompanied by substantial accumulation of starch in parenchymal cells of the phloem
physiological function
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role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Isozyme SUS1 is not required for the sucrose-ethanol transition in seedlings under low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Isozyme SUS4 is not required for the sucrose-ethanol transition in seedlings under low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia; role for sucrose synthase as part of the acclimation mechanism to anoxia in dicotyledons. Contribution of sucrose synthases to the fermentative metabolism linked to the ability to survive low-oxygen conditions. Sucrose synthase contributes to ethanol production under anoxia
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physiological function
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CsSUS3 participates in resisting hypoxic stress, mechanism analysis
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additional information
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roots of plants deficient in sucrose synthase root isozyme are colonized successfully by arbuscular myccorhizal fungi in a similar levelthan the wild-type plant roots
additional information
structure-function relationship analysis, overview
additional information
structure-function relationship analysis, overview
additional information
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structure-function relationship analysis, overview
additional information
structure-function relationship analysis, overview
additional information
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structure-function relationship analysis, overview
additional information
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structure-function relationship analysis, overview
additional information
structure-function relationship analysis, overview
additional information
structure-function relationship analysis, overview
additional information
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a triad of conserved homologous catalytic residues, Arg567, Lys572, and Glu663, in the family is functionally critical in the Nitrosomonas europaea sucrose synthase, structure homology modeling, overview
additional information
a triad of conserved homologous catalytic residues, Arg567, Lys572, and Glu663, in the family is functionally critical in the Nitrosomonas europaea sucrose synthase, structure homology modeling, overview
additional information
enzyme homology modeling and substrate docking using the crystal structure of Nitrosomonas europaea NeSuS1, PDB ID 4RBN, and the crystal structure of Arabidopsis AtSuS1, PDB ID 3S28, overview
additional information
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structure-function relationship analysis, overview
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additional information
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structure-function relationship analysis, overview
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additional information
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structure-function relationship analysis, overview
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additional information
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structure-function relationship analysis, overview
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additional information
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structure-function relationship analysis, overview
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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
sucrose + UDP
UDP-glucose + D-fructose
sucrose loaded into the phloem of a poplar leaf is used directly by sucrose synthase associated with various beta-glucan synthases in the stem for UDPglucose formation in the sink tissue, thereby conserving the high energy bond between glucose and fructose
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-
?
UDP-alpha-D-galactose + D-fructose
UDP + sucrose
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23% of the activity with UDP-alpha-D-glucose
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-
?
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-fructose 6-phosphate
UDP + sucrose 6-phosphate
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sucrose synthase plays an important role in sugar metabolism during sucrose accumulation in the coffee fruit
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-
?
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
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-
?
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
-
-
?
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
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
-
sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants
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-
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
-
-
?
ADP-glucose + D-fructose
ADP + sucrose
-
-
-
r
ADP-glucose + D-fructose
ADP + sucrose
-
-
ADP is the best acceptor substrate in sucrose cleavage
-
r
CDP-glucose + D-fructose
CDP + sucrose
-
-
-
r
GDP-glucose + D-fructose
GDP + sucrose
-
-
-
r
NDP-glucose + D-fructose
NDP + sucrose
-
-
-
r
NDP-glucose + D-fructose
NDP + sucrose
the enzyme prefers transferring glucose from ADP-glucose rather than UDP-glucose
-
-
r
TDP-glucose + D-fructose
TDP + sucrose
-
lower activity in sucrose cleavage
-
-
r
UDP + sucrose
UDP-glucose + D-fructose
-
under appropriate conditions, the enzyme participates in the in vitro mobilization of sucrose from tonoplast vesicles
-
-
?
UDP + sucrose
UDP-glucose + D-fructose
-
involved in sucrose metabolism
-
-
r
UDP + sucrose
UDP-glucose + D-fructose
-
major enzyme of sucrose synthesis
-
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
-
-
?
UDP + sucrose
UDP-glucose + D-fructose
-
also substrate: ADP
-
?
UDP + sucrose
UDP-glucose + D-fructose
-
with SS2-isozyme TDP is 57%, with SS1-isozyme 91% as effective as UDP
-
?
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
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
typical Michaelis-Menten behavior with respect to both UDP-glucose and D-fructose, no substrate inhibition at any UDP-glucose and D-fructose concentration tested
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
the level of sucrose synthase activity in the developing cotyledons of plant genotypes differing in seed size at 500 to 600 growing degree days is correlated with the final seed size at maturity
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
-
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
preferred substrates in both reaction directions
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
the binding of beta-fructopyranose involves residues from both the GT-BN and the GT-BC domains, including those in the E-X7-E motif
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
the enzyme preferentially functions in the direction of sucrose cleavage at most cellular condition, it also catalyzes the synthetic reaction
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
lower activity in sucrose cleavage
-
-
r
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
-
-
?
UDPglucose + D-fructose
UDP + sucrose
-
main substrate is UDPglucose
-
r
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
-
SuS is involved in the Suc to polysaccharides conversion. Glycogen content in an Anabaena sp. mutant strain with an insertion inactivation of susA was lower than in the wild type strain under diazotrophic conditions, while both glycogen and polysaccharides levels are higher in a mutant strain constitutively overexpressing susA
-
-
-
additional information
?
-
-
L-sorbose, 5-keto-D-fructose, D-tagatose, fructose 6-phosphate, levanbiose can replace fructose to a small extent, no glucosyl acceptors are D-xylulose, L-rhamnulose, D-glucoheptulose, D-mannoheptulose, turanose, inulobiose, melibiulose, lactulose, cellobiulose, 3,4-di-O-methylfructose, dihydroxyacetone, pyruvate
-
-
-
additional information
?
-
-
it is supposed that the sucrose synthase activity in sugar-beet roots is controlled by sucrose synthesized in leaves rather than by phytohormones
-
-
-
additional information
?
-
-
sucrose synthase appears to be largely responsible for feeding assimilated carbon into sink metabolism
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
-
sucrose synthase affects carbon partitioning to increase cellulose production and altered cell wall ultrastructure, overview
-
-
-
additional information
?
-
-
nitrogen fixation can occur in Lotus japonicus nodules even in the absence of LjSUS3 (the major nodule-induced isoform of SUS), so LjSUS1 must also contribute to the maintenance of nitrogen assimilation
-
-
-
additional information
?
-
-
results support the model that nodule-enhanced Suc synthase 1 of the model legume Medicago truncatula is required for the establishment and maintenance of an efficient N-fixing symbiosis
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
substrate specificities of recombinant wild-type and mutant enzymes expressed in Escherichia coli or in Saccharomyces cerevisia, overview
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
UDP-glucose is preferred before ADP-glucose
-
-
-
additional information
?
-
-
unique nucleotide specificity of the sucrose synthase from Thermosynechococcus elongatus
-
-
-
additional information
?
-
-
sucrose synthase appears to be largely responsible for feeding assimilated carbon into sink metabolism
-
-
-
additional information
?
-
-
it is possible that sucrose synthase provides monosaccharide precursors for mucilage synthesis
-
-
-
additional information
?
-
-
sucrose synthase appears to be largely responsible for feeding assimilated carbon into sink metabolism. SH1 isozyme preferentially provides the substrate for cellulose biosynthesis, whereas SUS1 generates precursors for starch biosynthesis
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
sucrose + UDP
UDP-glucose + D-fructose
Q01390
sucrose loaded into the phloem of a poplar leaf is used directly by sucrose synthase associated with various beta-glucan synthases in the stem for UDPglucose formation in the sink tissue, thereby conserving the high energy bond between glucose and fructose
-
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + sucrose 6-phosphate
-
sucrose synthase plays an important role in sugar metabolism during sucrose accumulation in the coffee fruit
-
-
?
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
-
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
Q7Y078
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
-
-
?
NDP-glucose + D-fructose
NDP + sucrose
F4K5W8, P49040, Q00917, Q9FX32, Q9LXL5, Q9M111
-
-
-
r
UDP + sucrose
UDP-glucose + D-fructose
-
under appropriate conditions, the enzyme participates in the in vitro mobilization of sucrose from tonoplast vesicles
-
-
?
UDP + sucrose
UDP-glucose + D-fructose
-
involved in sucrose metabolism
-
-
r
UDP + sucrose
UDP-glucose + D-fructose
-
major enzyme of sucrose synthesis
-
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
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
F4K5W8, P49040, Q00917, Q9FX32, Q9LXL5, Q9M111
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
F4K5W8, P49040, Q00917, Q9FX32, Q9LXL5, Q9M111
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
F4K5W8, P49040, Q00917, Q9FX32, Q9LXL5, Q9M111
-
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
the level of sucrose synthase activity in the developing cotyledons of plant genotypes differing in seed size at 500 to 600 growing degree days is correlated with the final seed size at maturity
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
H6TFZ4, P30298, P31924, Q10LP5, Q43009, Q6K973
-
-
-
?
UDP-glucose + D-fructose
UDP + sucrose
Q43009
preferred substrates in both reaction directions
-
-
r
UDP-glucose + D-fructose
UDP + sucrose
-
the enzyme preferentially functions in the direction of sucrose cleavage at most cellular condition, it also catalyzes the synthetic reaction
-
-
r
additional information
?
-
-
SuS is involved in the Suc to polysaccharides conversion. Glycogen content in an Anabaena sp. mutant strain with an insertion inactivation of susA was lower than in the wild type strain under diazotrophic conditions, while both glycogen and polysaccharides levels are higher in a mutant strain constitutively overexpressing susA
-
-
-
additional information
?
-
-
it is supposed that the sucrose synthase activity in sugar-beet roots is controlled by sucrose synthesized in leaves rather than by phytohormones
-
-
-
additional information
?
-
-
sucrose synthase appears to be largely responsible for feeding assimilated carbon into sink metabolism
-
-
-
additional information
?
-
-
sucrose synthase affects carbon partitioning to increase cellulose production and altered cell wall ultrastructure, overview
-
-
-
additional information
?
-
-
nitrogen fixation can occur in Lotus japonicus nodules even in the absence of LjSUS3 (the major nodule-induced isoform of SUS), so LjSUS1 must also contribute to the maintenance of nitrogen assimilation
-
-
-
additional information
?
-
-
results support the model that nodule-enhanced Suc synthase 1 of the model legume Medicago truncatula is required for the establishment and maintenance of an efficient N-fixing symbiosis
-
-
-
additional information
?
-
-
sucrose synthase appears to be largely responsible for feeding assimilated carbon into sink metabolism
-
-
-
additional information
?
-
-
it is possible that sucrose synthase provides monosaccharide precursors for mucilage synthesis
-
-
-
additional information
?
-
-
sucrose synthase appears to be largely responsible for feeding assimilated carbon into sink metabolism. SH1 isozyme preferentially provides the substrate for cellulose biosynthesis, whereas SUS1 generates precursors for starch biosynthesis
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme exists as monophosphorylated and multiphosphorylated form, multiphopsphorylation increases affinity for UDP up to threefold
-
additional information
Ser11 is primary phosphorylation site, phosphorylation does not affect kinetics but partitioning between membrane and cytosol
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
NaCl
the transcript level and protein abundance of CsSUS3 hardly change during salinity treatment, but the enzyme activity increased slightly, especially on the first and ninth days, compared with control
additional information
Ca2+
-
activation of sucrose synthesis; slight activation of sucrose cleavage at 10 mM
Mg2+
-
activates incoporation of the enzyme into the cellulose synthase particles
additional information
-
no activation by K+, Na+, NH4+, Cl-, Br-, F-, NO3-, phosphate, sulfate, borate, acetate, citrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-Dimethylaminopurine
-
sucrose-induced activity of sucrose synthase is strongly inhibited by okadaic acid and less by 6-dimethylaminopurine at early stages of regeneration, but not at the stages preceding DNA replication or mitotic activities
GDP
substrate inhibition occurs in the presence of GDP at concentrations above 10 mM
okadaic acid
-
sucrose-induced activity of sucrose synthase is strongly inhibited by okadaic acid and less by 6-dimethylaminopurine at early stages of regeneration, but not at the stages preceding DNA replication or mitotic activities
D-fructose
-
mixed inhibitor with regard to both sucrose and UDP, substrate inhibition
UDP-glucose
-
competitive with respect to UDP and mixed inhibitor with respect to sucrose; substrate inhibition
additional information
-
typical Michaelis-Menten behavior with respect to both UDP-glucose and D-fructose, no substrate inhibition at any UDP-glucose and D-fructose concentration tested
-
additional information
-
decrease of enzyme activity in degrading direction in leaves during fruit development
-
additional information
-
not inhibitory: DTT, GSH, 2-mercaptoethanol, EDTA; not inhibitory: fructose 6-phosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 1,6-diphosphate; not inhibitory: galactose, mannose, maltose, raffinose, 3-phosphoglycerate, phosphoenolpyruvate, ethanol, succinate, 2-oxoglutarate, glutamine, NAD+, diphosphate
-
additional information
-
not inhibitory: cAMP; not inhibitory: fructose 2,6-diphosphate; not inhibitory: fructose 6-phosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 1,6-diphosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
as well as treatments like spikelet thinning, leaf cutting increase enzyme expression and enzyme activity during rice grain filling
nitrate
-
50% activation at 3-5 mM, exogenous nitrate at 14.2 mM absorbed in the form of KNO3 and Ca(NO3)2 during 10-20 days exponentially activates the enzyme in the roots by 22-100% as compared with plants grown on nitrogen-free medium. Under low light, nitrate can not activate sucrose synthase
Sucrose
-
exogenous, as well as treatments like spikelet thinning, leaf cutting increase enzyme expression and enzyme activity during rice grain filling
additional information
-
increase of enzyme activity in synthezising direction in leaves during fruit development, increase of enzyme activity in synthezising and in degrading direction in mesocarp tissue during fruit development
-
additional information
-
when suffering hypoxia stress from flooding, CsSUS3 expression and SUS activity in roots increase, especially in the lateral roots. The soluble SUS activity increases, but the membrane fraction hardly changes
-
additional information
when suffering hypoxia stress from flooding, CsSUS3 expression and SUS activity in roots increase, especially in the lateral roots. The soluble SUS activity increases, but the membrane fraction hardly changes
-
additional information
-
peak of activities at the 21th day post anthesis, higher activity in the cultivar with a high starch content
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
D-fructose
recombinant enzyme expressed in Saccharomyces cerevisiae
5.6
D-fructose
-
pH 7.0, 37°C, recombinant enzyme, with ADP-glucose
12
D-fructose
-
pH 7.0, 37°C, recombinant enzyme, with UDP-glucose
0.6
UDP-alpha-D-glucose
recombinant enzyme expressed in Saccharomyces cerevisiae
1.4
UDP-alpha-D-glucose
recombinant enzyme expressed in Escherichia coli
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics, except for GDP
-
additional information
additional information
Michaelis-Menten kinetics, except for GDP
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6
Sucrose
Thermosynechococcus elongatus
-
pH 7.0, 37°C, purified recombinant enzyme, with ADP in sucrose cleavage
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
D-fructose
Thermosynechococcus elongatus
-
pH 7.0, 37°C, recombinant enzyme, with UDP-glucose
117
0.406
D-fructose
Thermosynechococcus elongatus
-
pH 7.0, 37°C, recombinant enzyme, with ADP-glucose
117
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.003
-
value about, degrading direction, leaf, 20 days after anthesis; value about, synthezising direction, leaf, 2 days before anthesis
0.005
-
value about, degrading direction, leaf, 16 days after anthesis; value about, synthezising direction, leaf, 16 days after anthesis
0.0067
-
value about, degrading direction, leaf, 12 days after anthesis; value about, synthezising direction, leaf, 20 days after anthesis; value about, synthezising direction, mesocarp tissue, 16 days after anthesis
0.0083
-
value about, degrading direction, leaf, 4 days and 8 days after anthesis; value about, synthezising direction, mesocarp tissue, 20 days after anthesis; value about, synthezising direction, mesocarp tissue, 2 days before anthesis
0.01
0.0125
-
value about, degrading direction, leaf, 2 days before anthesis; value about, synthezising direction, mesocarp tissue, 8 days after anthesis
0.013
-
value about, synthezising direction, mesocarp tissue, day of anthesis
0.1
-
value about, degrading direction, mesocarp tissue, 2 days before anthesis and day of anthesis
0.1167
-
value about, degrading direction, mesocarp tissue, 4 days after anthesis
0.183
-
value about, degrading direction, mesocarp tissue, 8 days after anthesis
0.2083
-
value about, synthezising direction, mesocarp tissue, 12 to 20 days after anthesis
0.45
-
SUS activity in rice grain treated with abscisic acid during grain filling
0.53
-
SUS activity in rice grain treated with sducrose and abscisic acid during grain filling
6.9
purified recombinant enzyme, expressed in Saccharomyces cerevisiae
additional information
0.01
-
value about, degrading direction, leaf, day of anthesis; value about, synthezising direction, mesocarp tissue, 12 days after anthesis
additional information
-
the level of sucrose synthase activity in the developing cotyledons of plant genotypes differing in seed sizeat 500 to 600 growing degree days is correlated with the final seed size at maturity
additional information
-
specific activities in engineered and wild-type lines, the first show higher activities, in nmol/min x g FW
additional information
-
SuSy activity: 90 mU/g FW in wild-type tubers, 170-250 mU/g FW in transgenic overexpressing tubers
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.4
6.5
6.5
7.5
8.5
additional information
5
assay at; assay at; assay at; assay at; assay at; assay at
7
-
recombinant isoforms SUS1 and SUS3; recombinant isoforms SUS1 and SUS3
7.5
assay at; assay at; assay at; assay at; assay at; assay at; assay at
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.2
-
about 90% of maximal activity at pH 5.0 and about half-maximal activity at pH 8.2, sucrose cleavage
5.5 - 7.5
5.5 - 9
-
about 80% of maximal activity at pH 5.5 and about half-maximal activity at pH 9.0, sucrose cleavage
5.5 - 7.5
over 40% of maximal enzyme activity within this range
5.6 - 10
-
about half-maximal activity at pH 5.6 and about 90% of maximal activity at pH 10.0, sucrose synthesis
7 - 9
-
sucrose cleavage, activities with CDP, GDP, TDP, and UDP only occur at pH 7.0-8.0 and are very low at pH 9.0, while the activity with ADP is highest at pH 8.0 and higher than 60% of maximal activity in the pH range of 7.0-9.0
7.5 - 10
-
about half-maximal activity at pH 7.5 and about 90% of maximal activity at pH 10.0, sucrose synthesis
9.5
-
about 10-15% of maximum activity; about 10-15% of maximum activity
5.5 - 7.5
over 40% of maximal enzyme activity within this range
5.5 - 7.5
over 40% of maximal enzyme activity within this range
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
50
pH 6.5, cleavage of sucrose, SuSyI. Synthesis of sucrose, SuSy II
55
60
70
37
assay at; assay at; assay at; assay at; assay at; assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
total protein extract shows two cross-reacting spots at 88000 Da with a pI of 5.5 to 6.0
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
at 3 d and 10 d after flowering, SUS protein localized to the silique wall, seed coat, funiculus, and endosperm. By 13 d after flowering, SUS protein is detected in the embryo and aleurone layer, but is absent from the seed coat and funiculus
-
CaSUS1 expression is barely detectable in young flower buds and leaves. Transcripts of this isoform are observed in old flower buds and roots, and accumulates to a high level in stems
-
at least one form of SuSy present in young tissue is absent, or present below detection limits, in mature culm tissue
-
at 3 d and 10 d after flowering, SUS protein localized to the silique wall, seed coat, funiculus, and endosperm. By 13 d after flowering, SUS protein is detected in the embryo and aleurone layer, but is absent from the seed coat and funiculus
expressed at high levels during secondary cell wall synthesis in fiber
-
SUS1 is the predominant isoform of SUS associated with microsomes isolated from the base of the maize leaf elongation zone and from kernels at 20 and 30 days after pollination. SUS2 exists predominantly as a hetero-oligomer with SUS1 in kernels; SUS2 is particularly abundant in kernels at various pollination stages; SUSSH1 is predominant in developing kernels
-
; mRNA levels of CaSUS2 is barely detectable in young pericarp, but increased towards the ripening of pericarp tissues
-
at 3 d and 10 d after flowering, SUS protein localized to the silique wall, seed coat, funiculus, and endosperm. By 13 d after flowering, SUS protein is detected in the embryo and aleurone layer, but is absent from the seed coat and funiculus
-
at 3 d and 10 d after flowering, SUS protein localized to the silique wall, seed coat, funiculus, and endosperm. By 13 d after flowering, SUS protein is detected in the embryo and aleurone layer, but is absent from the seed coat and funiculus. Within the silique wall, SUS localizes specifically to the companion cells, indicating that SUS activity may be required to provide energy for phloem transport activities in the silique wall
additional information
-
developing, sucrose synthase reaches a maximum about 500 to 600 growing degree days after flowering, when cell numbers were no longer increasing, but the cotyledons are increasing rapidly in dry weight
-
at 3 d and 10 d after flowering, SUS protein localized to the silique wall, seed coat, funiculus, and endosperm. By 13 d after flowering, SUS protein is detected in the embryo and aleurone layer, but is absent from the seed coat and funiculus
-
mRNA levels of CaSUS2 is undetectable in young endosperm, but increased towards the ripening of endosperm tissues
-
CaSUS1 expression is barely detectable in young flower buds and leaves. Transcripts of this isoform are observed in old flower buds and roots, and accumulates to a high level in stems; CaSUS2 expression is low in flower buds and in flowers whether young or mature
-
CaSUS1 mRNAs accumulats mainly during the early development of perisperm and endosperm, as well as during pericarp growing phases; CaSUS2 transcript levels is maximal at later stages of pericarp (205234 day after flowering) and endosperm (234 day after flowering) development. Weak CaSUS2 expression is observed in the early stages (60 and 89 day after flowering) of perisperm development, as well as at 176 day after flowering
-
very low enzyme activity in young and unripe muskmelons, but rapid accumulation of sucrose during ripening
-
SuSy activity increases dramatically during fruit maturation, while activity is low at the young fruit developmental stage, still lower at the endocarp hardening stage
in green fruit, isoform Sus4 is expressed at nearly 200fold lower levels than isoform Sus3. Elevated level of expression in ripening fruit for isoform Sus3; in green fruit, isoform Sus4 is expressed at nearly 200fold lower levels than sioform Sus3
enzymic activity is higher in immature internodes than in mature internodes in all cultivars, sucrose synthase transcript expression shows a similar pattern. Sucrose synthase activity is negatively correlated with sucrose and positively correlated with hexose sugars
-
level can differ significantly in different parts of the internodes and with maturity. Both vascular and storage parenchyma tissue contain SuSy in young and mature internodes
isozyme expresssion patterns during development differ from each other; isozyme expresssion patterns during development differ from each other; isozyme expresssion patterns during development differ from each other; isozyme expresssion patterns during development differ from each other; isozyme expresssion patterns during development differ from each other; isozyme expresssion patterns during development differ from each other
Arachnis hookeriana x Ascocenda Madame Kenny
-
high expression of Msus1 mRNA in expanding leaves, not detectable in expanding leaves
-
2 genotypes ICPL 84023 and ICP 301 tolerant to waterlogging stress, and 2 genotypes ICP 7035 and Pusa 207 susceptible to waterlogging stress. Pattern of variation in reducing sugar content in the 4 genotypes is parallel to sucrose synthase activity. ICPL 84023 and ICP 301 also show fewer declines in total and non-reducing sugars and greater increase in reducing sugar and SuSy activity than ICP 7035 and Pusa 207
-
high CaSUS2 gene expression is observed in light-exposed leaves (positioned at the terminal ending of the branch). CaSUS2 mRNA levels is moderate in shaded leaves (collected inside the plant)
; developing; developing, SUS1
-
low expression enzyme level in young leaves, moderate levels in old leaves
-
elongation zone, isoenzyme SUS2. SUS2 exists predominantly as a hetero-oligomer with SUS1 in kernels; elongation zone, isoenzyme SUS-SH1; SUS1 is the predominant isoform of SUS associated with microsomes isolated from the base of the maize leaf elongation zone and from kernels at 20 and 30 days after pollination
-
light and metabolic signals control the selective degradation of sucrose synthase in maize leaves during deetiolation. SUS degradation is important to supply residues for the synthesis of other proteins required for autotrophic metabolism
isozyme SUS1; isozyme SUS4
-
activity of sucrose synthase and the content of starch in the xylem and phloem of the two birch varieties, 40-year-old trees, and 8-year-old trees of Betula carelica, overview
-
SuSy is specifically localized in the creous walled sieve element of the phloem
-
sucrose synthase has a role in the construction of the extracellular matrix and thus in the morphogenesis of pollen tubes. Distribution of Sus is affected by brefeldin A and depended on the nutrition status of the pollen tube, because an absence of metabolic sugars in the growth medium caused Sus to distribute differently during tube elongation
-
it is supposed that the sucrose synthase activity in sugar-beet roots is controlled by sucrose synthesized in leaves rather than by phytohormones
-
activities of sucrose synthase is not significantly higher in wounded roots than in unwounded controls at any time during 13 days of postwounding storage
-
SBSS1 transcript levels are elevated in wounded, anoxic and cold-treated roots. SBSS1 protein levels exhibit little change in stressed roots, even after 7 d. SBSS1 expression in response to wounding, anoxia and cold may be regulated by post-transcriptional mechanisms; SBSS2 transcript levels are elevated in wounded, anoxic and cold-treated roots. SBSS2 protein levels exhibit little change in stressed roots, even after 7 d. SBSS2 expression in response to wounding, anoxia and cold may be regulated by post-transcriptional mechanisms
-
CaSUS1 expression is barely detectable in young flower buds and leaves. Transcripts of this isoform are observed in old flower buds and roots, and accumulates to a high level in stems; high CaSUS2 gene expression is observed in roots
enzyme localization in the cells of phloem region in vascular tissues
-
enzyme localization in the cells of phloem region in vascular tissues
-
-
an 80% to 90% reduction of MtSucS1 proteins in roots and root nodules specifically limit plant growth and organ development under nodulation-dependent conditions, leading to marked changes in expression of genes involved in the nodule C and N metabolism and consequently to a reduced performance of amino acid biosynthesis
isoform sus4 is expressed at nearly 200fold lower levels than sioform Sus3; isoform sus4 is expressed at nearly 200fold lower levels than sioform Sus3
-
increased activity is in the tip region and in the stele of root axes. Increased in situ activity correlates with cell wall thickening by cellulose deposition under hypoxia
-
sucrose synthase is one of the central enzymes in sucrose cleavage in root nodules; sucrose synthase is one of the central enzymes in sucrose cleavage in root nodules. SuSy2 is the second most abundant isoform present in Medicago truncatula root nodules
-
an 80% to 90% reduction of MtSucS1 proteins in roots and root nodules specifically limit plant growth and organ development under nodulation-dependent conditions, leading to marked changes in expression of genes involved in the nodule C and N metabolism and consequently to a reduced performance of amino acid biosynthesis
transcriptional and post-translational regulation of sucrose synthase in pea nodules by the cellular redox state
-
at 3 d and 10 d after flowering, SUS protein localized to the silique wall, seed coat, funiculus, and endosperm. By 13 day after flowering, SUS protein is detected in the embryo and aleurone layer, but is absent from the seed coat and funiculus. Co-localization of SUS protein and starch grains in the seed coat at 3 and 10 day after flowering indicates that SUS may be involved in temporary starch deposition during the early stages of seed development
-
sucrose synthase activity is increased in shoot tips of the transgenic apple plants with decreased sorbitol synthesis compared with the untransformed control
-
CaSUS1 expression is barely detectable in young flower buds and leaves. Transcripts of this isoform are observed in old flower buds and roots, and accumulates to a high level in stems; CaSUS2 mRNA levels is moderate in stems
elevated expression of isoform Sus4 in the higher, less mature portions of stem; isoform SUS3 expression is not significantly altered throughout the internodes
-
activity of sucrose synthase and the content of starch in the xylem and phloem of the two birch varieties, 40-year-old trees, and 8-year-old trees of Betula carelica, overview
additional information
nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview
additional information
nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview
additional information
nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview
additional information
nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview
additional information
nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview
additional information
nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview; nematode-induced syncytium in roots, isozymes expression analysis, overview
additional information
Arachnis hookeriana x Ascocenda Madame Kenny
-
expression of Msus1 mRNA is not detectable in flowers
additional information
-
transcript abundance of SBSS2, relative to SBSS1, is greater in young vegetative and floral tissues, and reduced in mature vegetative tissues
additional information
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
-
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
tissue-specific expression analysis; tissue-specific expression analysis; tissue-specific expression analysis, SUS2 is widely expressed in tissues; tissue-specific expression analysis, SUS3 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS4 is predominantly expressed in the caryopsis; tissue-specific expression analysis, SUS5 is widely expreesed in tissues at low level and is suppressed in germinating shoots under submergence; tissue-specific expression analysis, SUS6 is widely expressed in tissues at low levels and is suppressed in germinating shoots under submergence
additional information
-
tissue specific expression enzyme levels, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
inner side of cell membrane; inner side of cell membrane
-
-
tonoplast enzyme is approximately 7% of the total tissue activity
-
additional information
-
analysis by bidimensional electrophoresis indicates that Sus exists as two isoforms, one of which is phosphorylated and more abundant in the cytoplasm and cell wall and the other of which is not phosphorylated and is specific to the plasma membrane
within the cytoplasm and along cytoplasmic tracks; within the cytoplasm and along cytoplasmic tracks
-
SUS2 may be the housekeeping SUS isoform because it is solely cytosolic and therefore cleaves sucrose for metabolic requirements within the cytosol
-
a mechanism involving protein phosphorylation/dephosphorylation and/or calcium would in part control the association of the isoforms of sucrose synthase with membranes in developing fruit
-
SUS1 is associated with membranes; SUS-SH1 is associated with membranes
-
partial membrane localization when expressed in Escherichia coli. Two regions of SUS1 contribute to membrane affinity: the amino-terminal noncatalytic domain, and a region with sequence similarity to the C-terminal pleckstrin homology domain of human pleckstrin. Alanine substitutions within the pleckstrin homology-like domain of SUS1 reduce membrane association in Escherichia coli and with plant microsomes in vitro without reducing enzymatic activity
-
analysis by bidimensional electrophoresis indicates that Sus exists as two isoforms, one of which is phosphorylated and more abundant in the cytoplasm and cell wall and the other of which is not phosphorylated and is specific to the plasma membrane
-
of pollen tube, colocalization with callose synthase and cellulose synthase. Sucrose synthase binds to actin filaments depending on sucrose concentration. Its distribution within the plasma membrane is dependent on the actin cytoskeleton and the endomembrane system but not on microtubules
-
the plasma membrane-associated rosette anchors the catalytic unit of cellulose synthesis to form the functional cellulose synthesis machinery
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
86000
2 * 84000 + 2 * 86000, SuSyI, SDS-PAGE; 4 * 86000, SuSyII, SDS-PAGE
87000
88000
90000
94000
95000
320000
360000
380000
410000
420000
440000
540000
additional information
88000
-
4 * 88000, SDS-PAGE, depending on the ionic species and ionic strength of the solution, the enzyme can aquire catalytically active, tetrameric, octameric and other higher aggregated forms of which the tetramer is the predominant form
95000
4 * 95000, recombinant His-tagged enzyme, SDS-PAGE, each monomer contains four domains, i.e. SSN-1, SSN-2, GT-B(A), and GT-B(D), structure overview and comparisons
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
oligomer
tetramer
additional information
?
x * 92200, calculated; x * 92300, calculated; x * 98700, calculated
homotetramer
4 * 95000, recombinant His-tagged enzyme, SDS-PAGE, each monomer contains four domains, i.e. SSN-1, SSN-2, GT-B(A), and GT-B(D), structure overview and comparisons
tetramer
2 * 84000 + 2 * 86000, SuSyI, SDS-PAGE; 4 * 86000, SuSyII, SDS-PAGE
tetramer
-
4 * 88000, SDS-PAGE, depending on the ionic species and ionic strength of the solution, the enzyme can aquire catalytically active, tetrameric, octameric and other higher aggregated forms of which the tetramer is the predominant form
additional information
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
-
additional information
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
-
additional information
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
-
additional information
-
structure-function relationship analysis, overview
additional information
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
-
additional information
comparison of structure and active site of starch, glycogen, sucrose synthases
additional information
structure-function relationship analysis, overview
additional information
-
structure-function relationship analysis, overview
-
additional information
-
the enzyme forms the catalytic unit of the cellulose synthesis machinery as detergent-soluble granular particles enriched with a 78 kDa polypeptide of sucrose synthase, identification by mass spectrometry and immunoblotting. The catalytic units bind to plasma membrane-associated rosette structures and retain the cellulose synthesis activity in the presence of UDP-glucose or sucrose plus UDP when supplemented with magnesium, incorporation of the catalytic unit into the rosette structure, overview
additional information
-
SUS2 exists predominantly as a heterooligomer with SUS1; SUS2 predominantly exists as a hetero-oligomer with SUS1
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
analysis by bidimensional electrophoresis indicates that Sus exists as two isoforms, one of which is phosphorylated and more abundant in the cytoplasm and cell wall and the other of which is not phosphorylated and is specific to the plasma membrane
phosphoprotein
-
11 phosphorylation sites. The enzyme is largely dephosphorylated in fruits fed EDTA or staurosporine, compared to fruits fed water or sucrose
phosphoprotein
-
S170 phosphorylation promotes the formation of high molecular mass forms, ubiquitin/sucrose-synthase conjugates than can be targeted for 26S-proteasome-dependent degradation
phosphoprotein
-
phosphorylated at a C-terminal threonine residue only in midvein; phosphorylated at a C-terminal threonine residue only in midvein. SUS-SH1 is phosphorylated in vivo at the Ser10 site in kernels
phosphoprotein
-
calcium-dependent protein kinase-mediated phosphorylation of recombinant SUS1 at the Ser15 site is a negative regulator of its association with actin
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as a complex with UDP-glucose and as a complex with UDP and fructose, at 2.8- and 2.85 A resolution, respectively
-
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 15mg/ml protein solution with 0.001 ml of reservoir solution containing 5% Tacsimate, pH 5.0, 5% w/v PEG 3350, and 0.1 M sodium citrate, pH 5.6, 20°C, 7 days, X-ray diffraction structure determination and analysis at 3.05 A resolution, molecular replacement with Arabidopsis thaliana sucrose synthase structural model, PDB ID 3S29, as a template
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
the enzyme remains stable after 10 min incubation up to 50°C, but activity sharply decays beyond 55°C. Addition of 1 mM ADP, 10 mM UDP, or 200 mM Suc enhances the thermal stability by almost 5°C
55
-
pH 6.5: t1/2: 1 min, complete inactivation after 10 min, pH 8: 20% loss of activity after 1 min, 80% loss of activity within 10 min
60
60
purified recombinant His-tagged enzyme, without substrates, 15 min, 96% activity remaining
60
purified recombinant His-tagged enzyme, without substrates, 15 min, no activity remaining
60
purified recombinant His-tagged enzyme, without substrates, 15 min, 38% activity remaining
60
purified recombinant His-tagged enzyme, without substrates, 15 min, 54% activity remaining
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
EDTA, 0.1 mM, stabilizes
freeze-thawing inactivates
repeated freeze-thawing leads to slight decrease of activity, even in the presence of PMSF
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.1 mM EDTA and DTT, more than 50% of activity retained after 1 month
-
4°C, 20 mM potassium phosphate buffer, pH 7.0, 5 mM 2-mercaptoethanol, 4 weeks stable
-
4°C, prolonged storage leads to slight decrease of activity, even in the presence of PMSF
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from roots partially by dialysis and ultracentrifugation
native enzyme partially by gel filtration, ammonium sulfate fractionation, and dialysis
-
partial
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity
recombinant wild-type and mutant enzyes from Pichia pastris by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
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
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 genotypes ICPL 84023 and ICP 301 tolerant to waterlogging stress, and 2 genotypes ICP 7035 and Pusa 207 susceptible to waterlogging stress. Pattern of variation in reducing sugar content in the 4 genotypes is parallel to sucrose synthase activity. ICPL 84023 and ICP 301 also show fewer declines in total and non-reducing sugars and greater increase in reducing sugar and SuSy activity than ICP 7035 and Pusa 207
-
cloning of sucrose synthase gene fragments. Sorghum sucrose synthase gene fragment I shares homology with other cereal sucrose synthase at the exon positions 6, 7, 8, 9 and 10. Sorghum sucrose synthase fragment II shares homology from exon 2 to 6
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
gene CmSS1, DNA and amino acid sequence determination and analysis, RT-PCR, RACE, and real time PCR analysis
-
gene PsnSuSy2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant overexpression of poplar xylem sucrose synthase in Nicotiana tabacum via Agrobacterium tumefaciens-mediated transformation leads to a thickened cell wall and increased height of transgenic plants, phenotypic changes in PsnSusy2 transgenic lines. PsnSuSy2 expression levels and altered wood properties in stem segments from the different transgenic lines, real-time quantitative PCR analyses of tissues and transgenic lines, overview
-
gene ss2, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) using plasmid pNESS2
gene Sus, DNA and amino acid sequence determination and analysis, tissue-specific expression analysis
-
gene SUS1, expression analysis in various rice tissues using real-time quantitative RT-PCR; gene SUS2, expression analysis in various rice tissues using real-time quantitative RT-PCR; gene SUS3, expression analysis in various rice tissues using real-time quantitative RT-PCR; gene SUS4, expression analysis in various rice tissues using real-time quantitative RT-PCR; gene SUS5, expression analysis in various rice tissues using real-time quantitative RT-PCR; gene SUS6, expression analysis in various rice tissues using real-time quantitative RT-PCR
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
gene sus1, quantitative expression analysism, genotyping and phenotype-genotype relationship at different environmental conditions; gene sus1, quantitative expression analysism, genotyping and phenotype-genotype relationship at different environmental conditions; gene sus2, quantitative expression analysism, genotyping and phenotype-genotype relationship at different environmental conditions; gene sus4, quantitative expression analysism, genotyping and phenotype-genotype relationship at different environmental conditions; gene sus5, quantitative expression analysism, genotyping and phenotype-genotype relationship at different environmental conditions; gene sus6, quantitative expression analysism, genotyping and phenotype-genotype relationship at different environmental conditions
gene SUS3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree of plant SUS enzymes, real-time quantitative PCR enzyme expression analysis, antisense expression of SUS3 in Cucumber sativus plants transformed via Agrobacterium tumefaciens strain LBA4404
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
gene SuSy, quantitative real-time PCR in wild-type and transgenic plant leaves
-
gene SuSyAc, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene SuSyDa, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene SuSyMr, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene SuSyNe, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene SuSyTm, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Nicotiana tabacum cv. xanthi.transgenic plants expressing either gene under the control of a tandem repeat cauliflower mosaic virus 35S promoter (2*35S) or a xylem-localized 4CL promoter (4-coumarate:CoA ligase) are generated. SuSy has the potential to increase overall plant growth and thus increase the total cellulose yield attainable from an individual plant
-
overexpression of the Gossypium hirsutum SuSy gene under control of two promoters in hybrid poplar Populus alba x grandidentata leading to significantly increased SuSy enzyme activity in developing xylem and to increased secondary cell wall cellulose content
-
recombinant overexpression in leaves of Nicotiana tabacum cv. SR1 plants via transfection with Agrobacterium tumefaciens strain GV3013; recombinant overexpression in leaves of Nicotiana tabacum cv. SR1 plants via transfection with Agrobacterium tumefaciens strain GV3013; recombinant overexpression in leaves of Nicotiana tabacum cv. SR1 plants via transfection with Agrobacterium tumefaciens strain GV3013; recombinant overexpression in leaves of Nicotiana tabacum cv. SR1 plants via transfection with Agrobacterium tumefaciens strain GV3013; recombinant overexpression in leaves of Nicotiana tabacum cv. SR1 plants via transfection with Agrobacterium tumefaciens strain GV3013; recombinant overexpression in leaves of Nicotiana tabacum cv. SR1 plants via transfection with Agrobacterium tumefaciens strain GV3013
sus3, recombinant expression of wild-type and mutant enzymes in Pichia pastoris
the gene is artificially synthesized for optimal recombinant expression in Escherichia coli strain Tuner (DE3)
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abscisic acid, exogenous sucrose, as well as treatments like spikelet thinning, leaf cutting increase enzyme expression and enzyme activity during rice grain filling, determination of protein, overview
-
effects of hypoxia, anoxia, and submergence on expression of genes sus1 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus4 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus5 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus6 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of gene sus2 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of gene sus3 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview
enzyme activity increases by 20-200% for 10-20 days of plant growth in presence of (NH4)2SO4 as compared with the roots of plants growing without nitrogen, induction is higher under illumination by sunlight
-
enzymic activity is higher in immature internodes than in mature internodes in all cultivars, sucrose synthase transcript expression shows a similar pattern. Sucrose synthase activity is negatively correlated with sucrose and positively correlated with hexose sugars
expression of isoform SS1 is upregulated by anoxia and by cold temperatures; expression of isoform SS1 is upregulated by anoxia and by cold teperatures; expression of isoform SS3 is upregulated by water deprivation and by cold teperatures
root restriction treatment increases the enzyme expression, while it reduces cytochrome pathway, and alternative pathway respirations with reduced ATP content. The ratio of invertase/sucrose synthase activity is increased in the restricted roots together with a decrease in glucose content and an increase in fructose content
-
the transcript level and protein abundance of CsSUS3 hardly change during salinity treatment, but the enzyme activity increased slightly, especially on the first and ninth days, compared with control
transcript profiling shows that gene expression of AtSUS1 is upregulated in 3-day-old galls and laser-microdissected giant cells of Meloidogyne javanica; transcript profiling shows that gene expression of AtSUS4 is upregulated in 3-day-old galls and laser-microdissected giant cells of Meloidogyne javanica
under anoxia, the induction of SUS1 is stronger than that of SUS4; under anoxia, the induction of SUS1 is stronger than that of SUS4
when suffering hypoxia stress from flooding, CsSUS3 expression and SUS activity in roots increase, especially in the lateral roots. The soluble SUS activity increases, but the membrane fraction hardly changes. Drought stress modulated by PEG-6000 causes a transient and slight increase in CsSUS3 transcript level on the first and third days, but decreases similarly to control on the sixth and ninth days
effects of hypoxia, anoxia, and submergence on expression of genes sus1 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus4 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus5 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus6 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of gene sus2 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of gene sus3 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview
effects of hypoxia, anoxia, and submergence on expression of genes sus1 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus4 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus5 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of genes sus6 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of gene sus2 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview; effects of hypoxia, anoxia, and submergence on expression of gene sus3 in wild-type and in sus1, sus4, and sus1/sus4 mutants, overview
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the transcript level and protein abundance of CsSUS3 hardly change during salinity treatment, but the enzyme activity increased slightly, especially on the first and ninth days, compared with control
the transcript level and protein abundance of CsSUS3 hardly change during salinity treatment, but the enzyme activity increased slightly, especially on the first and ninth days, compared with control
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under anoxia, the induction of SUS1 is stronger than that of SUS4; under anoxia, the induction of SUS1 is stronger than that of SUS4
under anoxia, the induction of SUS1 is stronger than that of SUS4; under anoxia, the induction of SUS1 is stronger than that of SUS4
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when suffering hypoxia stress from flooding, CsSUS3 expression and SUS activity in roots increase, especially in the lateral roots. The soluble SUS activity increases, but the membrane fraction hardly changes. Drought stress modulated by PEG-6000 causes a transient and slight increase in CsSUS3 transcript level on the first and third days, but decreases similarly to control on the sixth and ninth days
when suffering hypoxia stress from flooding, CsSUS3 expression and SUS activity in roots increase, especially in the lateral roots. The soluble SUS activity increases, but the membrane fraction hardly changes. Drought stress modulated by PEG-6000 causes a transient and slight increase in CsSUS3 transcript level on the first and third days, but decreases similarly to control on the sixth and ninth days
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A642N
site-directed mutagenesis, the mutant shows unaltered Km for UDP compared to the wild-type enzyme
L636Q/A642N
site-directed mutagenesis, the mutant shows unaltered Km for UDP compared to the wild-type enzyme
L636Q/V641R/A642N
site-directed mutagenesis, the mutant shows unaltered Km for UDP compared to the wild-type enzyme
A642N
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site-directed mutagenesis, the mutant shows unaltered Km for UDP compared to the wild-type enzyme
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L636Q/A642N
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site-directed mutagenesis, the mutant shows unaltered Km for UDP compared to the wild-type enzyme
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L636Q/V641R/A642N
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site-directed mutagenesis, the mutant shows unaltered Km for UDP compared to the wild-type enzyme
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E678Q
site-directed mutagenesis, almost inactive mutant, the mutant shows impaired D-fructose binding
E686D
site-directed mutagenesis, the mutant enzyme retains 34.9% of sucrose cleavage and 37.9% of sucrose synthesis activity, respectively
E686Q
site-directed mutagenesis, inactive mutant, the mutant shows impaired D-fructose binding
F680S
site-directed mutagenesis, inactive mutant, the mutant shows impaired D-fructose binding
F680Y
site-directed mutagenesis, the mutant enzyme retains 61.0% of sucrose cleavage and all of sucrose synthesis activity, respectively
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
additional information
manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase
additional information
manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase
additional information
manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase
additional information
manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase
additional information
manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase
additional information
manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase; manipulation of sugar levels in transgenic plants by overexpressing sucrose synthase
additional information
generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines
additional information
generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines
additional information
generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines
additional information
generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines
additional information
generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines
additional information
generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines; generation and analysis of isozyme mutant lines
additional information
generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
additional information
generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
additional information
generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
additional information
generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
additional information
generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
additional information
generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
additional information
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generation of a sus1 mutant and a sus1/sus4 double mutant. None of the other five genes display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; generation of a sus4 mutant and a sus1/sus4 double mutant. Gene sus4 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene SUS2 does not display an altered pattern of expression as a consequence of the lack of SUS1; gene SUS3 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus5 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview; gene sus6 does not display an altered pattern of expression as a consequence of the lack of SUS1. Impact of SUS mutations on ethanol production and ATP/ADP ratio under low-oxygen conditions, overview
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additional information
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activity and specific activity of sucrose synthase in podwalls are significantly higher in genetically modified temperature-tolerant lines 5012, 5014 and 5039 compared to wild-type ICCV 96029 and 96030, overview
additional information
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antisense suppression of Cucumis sativus sucrose synthase 3 reduces hypoxic stress tolerance. Compared with the wild-type cucumbers, the transgenic lines with antisense expression of CsSUS3 are more sensitive to flooding. After 6 days of flooding, the enzyme activity, soluble sugar and UDP-glucose content and the ratio of ATP/ADP in the roots of transgenic plants are significantly lower than that in wild-type plants. The transgenic lines grow more slowly with more yellow necrosis in the leaves, phenotype overview
additional information
antisense suppression of Cucumis sativus sucrose synthase 3 reduces hypoxic stress tolerance. Compared with the wild-type cucumbers, the transgenic lines with antisense expression of CsSUS3 are more sensitive to flooding. After 6 days of flooding, the enzyme activity, soluble sugar and UDP-glucose content and the ratio of ATP/ADP in the roots of transgenic plants are significantly lower than that in wild-type plants. The transgenic lines grow more slowly with more yellow necrosis in the leaves, phenotype overview
additional information
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antisense suppression of Cucumis sativus sucrose synthase 3 reduces hypoxic stress tolerance. Compared with the wild-type cucumbers, the transgenic lines with antisense expression of CsSUS3 are more sensitive to flooding. After 6 days of flooding, the enzyme activity, soluble sugar and UDP-glucose content and the ratio of ATP/ADP in the roots of transgenic plants are significantly lower than that in wild-type plants. The transgenic lines grow more slowly with more yellow necrosis in the leaves, phenotype overview
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additional information
N-terminal truncation, phosphorylations still occurs, but weakly
additional information
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silencing of Sus expression in the endosperm by RNAi disrupts its cellularisation process and inhibits early seed development
additional information
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construction of trangenic antisense construct expressing plants, that display up to 10fold reduced SucS1 levels in roots anf reduced arbuscular mycorrhiza. Mycorrhizal MtSucS1-reduced lines exhibit an overall stunted aboveground growth under phosphorus limitation. The transgenic plants show, apart from a reduced plant height, shoot weight, and leaf development, a delayed flowering, resulting in a lower seed yield. In addition, the root-to-shoot and root weight ratios increase significantly. Major reversion of arbuscular mycorrhiza-associated transcription, exhibiting a significant repression of well-known plant arbuscular mycorrhiza marker and mycosymbiont genes, together indicating a diminished AM fungus colonization of MtSucS1-antisense lines, phenotype, overview
additional information
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overexpression of the Gossypium hirsutum SuSy gene under control of two promoters in hybrid poplar Populus alba x grandidentata leads to significantly increased SuSy enzyme activity in developing xylem and to increased secondary cell wall cellulose content
additional information
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root restriction treatment increases the enzyme expression, while it reduces cytochrome pathway, and alternative pathway respirations with reduced ATP content. The ratio of invertase/sucrose synthase activity is increased in the restricted roots together with a decrease in glucose content and an increase in fructose content
additional information
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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
additional information
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recombinant ectopic expression of the enzyme from Solanum tuberosum in Zea mays seed endosperm leads to transgenic developing seeds that 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, phenotype, overview. Enhancement of the enzyme activity does not affect the redox status of AGP
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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sucrose synthase is a good physiological indicator for use in breeding for improved seed size in chickpea
LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.13)
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