Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	4,023 proteins
Enzyme class ^help_outline	EC 2.4.1.14 sucrose-phosphate synthase
GO Molecular Function ^help_outline	GO:0046524 sucrose-phosphate synthase activity

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Name ^help_outline β-D-fructose 6-phosphate Identifier CHEBI:57634 (Beilstein: 6422468) ^help_outline Charge -2 Formula C6H11O9P InChIKey^help_outline BGWGXPAPYGQALX-ARQDHWQXSA-L SMILES^help_outline OC[C@@]1(O)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline UDP-α-D-glucose Identifier CHEBI:58885 (Beilstein: 3827329) ^help_outline Charge -2 Formula C15H22N2O17P2 InChIKey^help_outline HSCJRCZFDFQWRP-JZMIEXBBSA-L SMILES^help_outline OC[C@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 256 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline sucrose 6^F-phosphate Identifier CHEBI:57723 (Beilstein: 3918937) ^help_outline Charge -2 Formula C12H21O14P InChIKey^help_outline PJTTXANTBQDXME-UGDNZRGBSA-L SMILES^help_outline OC[C@H]1O[C@H](O[C@]2(CO)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]2O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKey^help_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILES^help_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 611 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:22172	RHEA:22173	RHEA:22174	RHEA:22175
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	4,023 proteins
EC numbers ^help_outline	2.4.1.14
Gene Ontology ^help_outline	GO:0046524
KEGG ^help_outline				R00766
MetaCyc ^help_outline		SUCROSE-PHOSPHATE-SYNTHASE-RXN

Publications

Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution.

Cumino A., Curatti L., Giarrocco L., Salerno G.L.

Based on the functional characterization of sucrose biosynthesis related protiens[SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species a ... >> More

Based on the functional characterization of sucrose biosynthesis related protiens[SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species and plants, and that they are multidomain proteins with modular architecture. Anabaena SPS, a minimal catalytic SPS unit, defines a glucosyltransferase domain present in all SPSs and SuSs. Similarly, Anabaena SPP defines a phosphohydrolase domain characteristic of all SPPs and some SPSs. Phylogenetic analysis points towards the evolution of modern cyanobacterial and plant SBP from a bidomainal common ancestral SPS-like gene. << Less

FEBS Lett 517:19-23(2002) [PubMed] [EuropePMC]
Sucrose-phosphate synthase from Synechocystis sp. strain PCC 6803: identification of the spsA gene and characterization of the enzyme expressed in Escherichia coli.

Curatti L., Folco E., Desplats P., Abratti G., Limones V., Herrera-Estrella L., Salerno G.

The first identification and characterization of a prokaryotic gene (spsA) encoding sucrose-phosphate synthase (SPS) is reported for Synechocystis sp. strain PCC 6803, a unicellular non-nitrogen-fixing cyanobacterium. Comparisons of the deduced amino acid sequence and some relevant biochemical pro ... >> More

The first identification and characterization of a prokaryotic gene (spsA) encoding sucrose-phosphate synthase (SPS) is reported for Synechocystis sp. strain PCC 6803, a unicellular non-nitrogen-fixing cyanobacterium. Comparisons of the deduced amino acid sequence and some relevant biochemical properties of the enzyme with those of plant SPSs revealed important differences in the N-terminal and UDP-glucose binding site regions, substrate specificities, molecular masses, subunit compositions, and regulatory properties. << Less

J Bacteriol 180:6776-6779(1998) [PubMed] [EuropePMC]
The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode.

Chua T.K., Bujnicki J.M., Tan T.C., Huynh F., Patel B.K., Sivaraman J.

Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central reg ... >> More

Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme. << Less

Plant Cell 20:1059-1072(2008) [PubMed] [EuropePMC]

RHEA:22172 beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = sucrose 6(F)-phosphate + UDP + H(+)

Enzymes

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Cross-references

Publications

Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution.

Sucrose-phosphate synthase from Synechocystis sp. strain PCC 6803: identification of the spsA gene and characterization of the enzyme expressed in Escherichia coli.

The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode.