Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline tomatidine Identifier CHEBI:166999 Charge 1 Formula C27H46NO2 InChIKeyhelp_outline XYNPYHXGMWJBLV-VXPJTDKGSA-O SMILEShelp_outline C1C[C@]2([C@@](CC[C@@]3([C@@]2(CC[C@@H](C3)O)C)[H])([C@]4([C@]1([C@@]5([C@](C4)(O[C@@]6([C@H]5C)[NH2+]C[C@@H](C)CC6)[H])[H])C)[H])[H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 1 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 tomatidine 3-O-β-D-glucopyranoside Identifier CHEBI:166998 Charge 1 Formula C33H56NO7 InChIKeyhelp_outline JDRMNHOIHYWSFN-UGSFAPCESA-O SMILEShelp_outline C1C[C@]2([C@@](CC[C@@]3([C@@]2(CC[C@@H](C3)O[C@H]4[C@@H]([C@H]([C@@H]([C@H](O4)CO)O)O)O)C)[H])([C@]5([C@]1([C@@]6([C@](C5)(O[C@@]7([C@H]6C)[NH2+]C[C@@H](C)CC7)[H])[H])C)[H])[H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 1 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:66284 | RHEA:66285 | RHEA:66286 | RHEA:66287 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Cloning and expression of solanidine UDP-glucose glucosyltransferase from potato.
Moehs C.P., Allen P.V., Friedman M., Belknap W.R.
A cDNA encoding solanidine glucosyltransferase (SGT) was isolated from potato. The cDNA was selected from a yeast expression library using a positive selection based on the higher toxicity of steroidal alkaloid aglycons relative to their associated glycosylated forms. The cDNA contained an open re ... >> More
A cDNA encoding solanidine glucosyltransferase (SGT) was isolated from potato. The cDNA was selected from a yeast expression library using a positive selection based on the higher toxicity of steroidal alkaloid aglycons relative to their associated glycosylated forms. The cDNA contained an open reading frame encoding a 56 kDa polypeptide with regions of similarity to previously characterized UDP-glucosyltransferases. The enzyme activity and reaction products of recombinant SGT in yeast were consistent with those observed for the endogenous enzyme from potato. SGT mRNA and protein accumulated in tubers in response to wounding. The time course for SGT mRNA accumulation paralleled that of 3-hydroxy-3-methylglutaryl-coenzymeA isoform 1 (hmg1) mRNA. Steady-state SGT mRNA levels also increased transiently upon wounding of leaves. << Less
Plant J. 11:227-236(1997) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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A novel glucosyltransferase involved in steroid saponin biosynthesis in Solanum aculeatissimum.
Kohara A., Nakajima C., Hashimoto K., Ikenaga T., Tanaka H., Shoyama Y., Yoshida S., Muranaka T.
Steroidal saponins are widely distributed in many plant species. Their diverse structures have resulted in a wide range of applications, including drug and medicine production. It has been suggested that the nature of the non-saccharide and oligosaccharide portions of the saponin molecule both con ... >> More
Steroidal saponins are widely distributed in many plant species. Their diverse structures have resulted in a wide range of applications, including drug and medicine production. It has been suggested that the nature of the non-saccharide and oligosaccharide portions of the saponin molecule both contribute to the properties of individual saponins. Despite numerous studies on the occurrence, chemical structure, and varying pharmaceutical activities of steroidal saponins, their biosynthesis pathway is poorly understood. Glycosylation is thought to be the final step in steroidal saponin biosynthesis and it is thought to be involved in regulating the biological activities of saponins. Isolation of the glycosyltransferases that catalyze the transfer of sugar molecules to steroidal compounds will help to clarify the mechanisms that produce diverse saponins and control their activities in plants. In this study, we obtained three cDNAs encoding putative glycosyltransferases from Solanum aculeatissimum. One of the three, SaGT4A showed UDP-glucosyltransferase activity. This is the first cloned glucosyltransferase involved in steroidal saponin biosynthesis. SaGT4A catalyzes the 3-O-glucosylation of steroidal sapogenins, such as diosgenin, nuatigenin, and tigogenin. This enzyme also glucosylates steroidal alkaloids, such as solanidine, solasodine, and tomatidine. Gene expression analysis revealed that the accumulation of SaGT4A transcripts showed a unique response to wounding stress indicating the involvement of SaGT4A in plant defense system. << Less
Plant Mol. Biol. 57:225-239(2005) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
Comments
Published in: Stapleton A., Allen P.V., Friedman M. and Belknap W.R. Purification and characterization of solanidine glucosyltransferase from the potato (