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{{Sandbox_Reserved_ESBS_2015}}
{{Sandbox_Reserved_ESBS_2015}}
==Structure and Functional aspects of Sucrose Synthase from ''Arabidopsis thaliana''==
==Structure and Functional aspects of Sucrose Synthase from ''Arabidopsis thaliana''==
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Sucrose Synthase 1 (EC:2.4.1.13), also known as the Sucrose-UDP glucolsyltransferase 1 or simply Susy, is a reversible enzyme allowing the synthesis or the degradation of Sucrose in ''Arabidopsis thaliana''. It belongs to the Glycosyltransferase family 4 (GT4).
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Sucrose Synthase 1 (EC:2.4.1.13), also known as the Sucrose-UDP glucolsyltransferase 1 or simply Susy, is a reversible enzyme allowing the synthesis or the degradation of Sucrose in ''Arabidopsis thaliana''. It belongs to the Glycosyltransferase subfamily 4 (GT4).
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<StructureSection scene='71/719877/Susy/3' size='340' side='right' caption='X-ray crystal structures of AtSus1, as a complex with UDP-glucose at 2.8-Å resolution and as a complex with UDP and fructose at 2.85-Å resolution'>
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<StructureSection scene='' size='340' side='right' caption='X-ray crystal structures of AtSus1, as a complex with UDP-glucose at 2.8-Å resolution and as a complex with UDP and fructose at 2.85-Å resolution'>
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71/719877/Susy/3
== Function ==
== Function ==
The Sucrose Synthase is able to catalyse the following reaction in both directions:
The Sucrose Synthase is able to catalyse the following reaction in both directions:
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'''sucrose = glucose + fructose'''
 
[[Image:Susy_reaction.jpg]]
[[Image:Susy_reaction.jpg]]
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• 1-127: N-Terminal regulatory domain involved in targeting <ref>Determination of structural requirements and probable regulatory effectors for membrane association of maize sucrose synthase 1. Hardin SC, Duncan KA, Huber SC. Plant Physiol. 2006</ref>. On this sequence, two serines can be phosphorylated, which enable a control of enzyme location <ref>Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis. Hardin SC, Tang GQ, Scholz A, Holtgraewe D, Winter H, Huber SC. Plant J. 2003</ref>.
• 1-127: N-Terminal regulatory domain involved in targeting <ref>Determination of structural requirements and probable regulatory effectors for membrane association of maize sucrose synthase 1. Hardin SC, Duncan KA, Huber SC. Plant Physiol. 2006</ref>. On this sequence, two serines can be phosphorylated, which enable a control of enzyme location <ref>Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis. Hardin SC, Tang GQ, Scholz A, Holtgraewe D, Winter H, Huber SC. Plant J. 2003</ref>.
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• 157-276: ENOD40 peptide-binding domain.
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• 1-127: CTD: Cellular targeting domain
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• 277-776 : GT-B glycosyltransferase domain.
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• 157-276: EPBD: ENOD40 peptide-binding domain. This domain has a role in the regulation of the enzyme.
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• 776-808 : C-terminal domain. The length of this domain is variable depending of the SUS isoform.
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• 277-776 : GT-B glycosyltransferase domain. It contains the catlytic site.
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• 776-808 : C-terminal extension. The length of this domain is variable depending of the SUS isoform.
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[[Image:Monomer_structure.jpg]]
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== Structural highlights ==

Revision as of 11:53, 30 January 2016

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Structure and Functional aspects of Sucrose Synthase from Arabidopsis thaliana

Sucrose Synthase 1 (EC:2.4.1.13), also known as the Sucrose-UDP glucolsyltransferase 1 or simply Susy, is a reversible enzyme allowing the synthesis or the degradation of Sucrose in Arabidopsis thaliana. It belongs to the Glycosyltransferase subfamily 4 (GT4).

X-ray crystal structures of AtSus1, as a complex with UDP-glucose at 2.8-Å resolution and as a complex with UDP and fructose at 2.85-Å resolution

Drag the structure with the mouse to rotate


References

• UniProt entry: P49040

• Brenda entry : 2.4.1.13

  1. ↑ Salerno GL, Curatti L Origin of sucrose metabolism in higher plants: when, how and why? Trends Plant Sci. 2003 Feb
  2. ↑ Baroja-Fernández, E., Muñoz, F.J., Saikusa, T., Rodríguez-López, M., Akazawa, T. and Pozueta-Romero, J. Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants. Plant Cell Physiol.
  3. ↑ Salerno GL, Curatti L. Origin of sucrose metabolism in higher plants: when, how and why? Trends Plant Sci. 2003 Feb
  4. ↑ Determination of structural requirements and probable regulatory effectors for membrane association of maize sucrose synthase 1. Hardin SC, Duncan KA, Huber SC. Plant Physiol. 2006
  5. ↑ Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis. Hardin SC, Tang GQ, Scholz A, Holtgraewe D, Winter H, Huber SC. Plant J. 2003
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