Enzymes
| Enzyme class help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline D-fructose Identifier CHEBI:37721 (Beilstein: 1680728; CAS: 57-48-7) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline RFSUNEUAIZKAJO-VRPWFDPXSA-N SMILEShelp_outline OC[C@H]1OC(O)(CO)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 26 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 InChIKeyhelp_outline HSCJRCZFDFQWRP-JZMIEXBBSA-L SMILEShelp_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 231 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sucrose Identifier CHEBI:17992 (CAS: 57-50-1) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline CZMRCDWAGMRECN-UGDNZRGBSA-N SMILEShelp_outline OC[C@H]1O[C@H](O[C@]2(CO)O[C@H](CO)[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 27 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 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_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 577 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 InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:55092 | RHEA:55093 | RHEA:55094 | RHEA:55095 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants.
Baroja-Fernandez E., Munoz F.J., Saikusa T., Rodriguez-Lopez M., Akazawa T., Pozueta-Romero J.
By using barley seeds, developmental changes of ADPglucose (ADPG)-producing sucrose synthase (SS) and ADPG pyrophosphorylase (AGPase) have been compared with those of UDPglucose (UDPG), ADPG, sucrose (Suc) and starch contents. Both ADPG-synthesizing SS and AGPase activity patterns were found to co ... >> More
By using barley seeds, developmental changes of ADPglucose (ADPG)-producing sucrose synthase (SS) and ADPG pyrophosphorylase (AGPase) have been compared with those of UDPglucose (UDPG), ADPG, sucrose (Suc) and starch contents. Both ADPG-synthesizing SS and AGPase activity patterns were found to correlate well with those of ADPG and starch contents. Remarkably, however, maximal activities of ADPG-synthesizing SS were found to be several fold higher than those of AGPase throughout seed development, the highest rate of starch accumulation being well accounted for by SS. Kinetic analyses of SS from barley endosperms and potato tubers in the Suc cleavage direction showed similar K(m) values for ADP and UDP, whereas apparent affinity for Suc was shown to be higher in the presence of UDP than with ADP. Moreover, measurements of transglucosylation activities in starch granules incubated with purified SS, ADP and [U-(14)C]Suc revealed a low inhibitory effect of UDP. The ADPG and UDPG contents in the transgenic S-112 SS and starch deficient potato mutant [Zrenner et al. (1995) Plant J. 7: 97] were found to be 35% and 30% of those measured in wild-type plants, whereas both glucose-1-phosphate and glucose-6-phosphate contents were found to be normal as compared with those of wild-type plants. The overall results thus strongly support a novel gluconeogenic mechanism reported previously [Pozueta-Romero et al. (1999) CRIT: Rev. Plant Sci. 18: 489] wherein SS catalyses directly the de novo production of ADPG linked to starch biosynthesis in heterotrophic tissues of plants. << Less
Plant Cell Physiol. 44:500-509(2003) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
-
Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence.
Porchia A.C., Curatti L., Salerno G.L.
The pathway of sucrose metabolism in cyanobacteria is just starting to be elucidated. The present study describes the first isolation and biochemical characterization of a prokaryotic sucrose synthase (SS, EC 2.4.1.13). Two SS forms (SS-I and SS-II) were detected in Anabaena sp. strain PCC 7119. T ... >> More
The pathway of sucrose metabolism in cyanobacteria is just starting to be elucidated. The present study describes the first isolation and biochemical characterization of a prokaryotic sucrose synthase (SS, EC 2.4.1.13). Two SS forms (SS-I and SS-II) were detected in Anabaena sp. strain PCC 7119. The isoform SS-II was purified 457-fold and its amino-terminal portion sequenced. Substrate specificity, kinetic constants, native protein and subunit molecular masses, and the effect of different ions and metabolites were studied for SS-II. Anabaena SS was shown to be a tetramer with a 92-kDa polypeptide that was recognized by maize SS polyclonal antibodies. Some striking differences from plant enzymes were demonstrated with respect to substrate affinities, regulation by metal ions and ATP, and the amino-acid sequence of the N-terminal region. << Less
Planta 210:34-40(1999) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.