Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline solasodine Identifier CHEBI:145043 Charge 1 Formula C27H44NO2 InChIKeyhelp_outline KWVISVAMQJWJSZ-VKROHFNGSA-O SMILEShelp_outline [C@]12([C@]3([C@@]([C@@]4(C(C[C@@H](O)CC4)=CC3)C)(CC[C@]2(C)[C@]5([C@@H]([C@]6(O[C@]5(C1)[H])CC[C@@H](C)C[NH2+]6)C)[H])[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 solasodine 3-β-D-glucoside Identifier CHEBI:145042 Charge 1 Formula C33H54NO7 InChIKeyhelp_outline XMLLJGHZPHTUKK-GAMIEDRGSA-O SMILEShelp_outline [H][C@]12C[C@@]3([H])[C@]4([H])CC=C5C[C@H](CC[C@]5(C)[C@@]4([H])CC[C@]3(C)[C@@]1([H])[C@H](C)[C@@]1(CC[C@@H](C)C[NH2+]1)O2)O[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O 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:61844 | RHEA:61845 | RHEA:61846 | RHEA:61847 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Molecular cloning and characterization of one member of 3beta-hydroxy sterol glucosyltransferase gene family in Withania somnifera.
Sharma L.K., Madina B.R., Chaturvedi P., Sangwan R.S., Tuli R.
Sterol glycosides are constituents of plant cell membranes. Glucosylations of the sterols are catalyzed by sterol glucosyltransferases (SGTs), which are members of family 1 glycosyltransferases. We have identified the family of SGT genes expressed in the leaves of a medicinal plant Withania somnif ... >> More
Sterol glycosides are constituents of plant cell membranes. Glucosylations of the sterols are catalyzed by sterol glucosyltransferases (SGTs), which are members of family 1 glycosyltransferases. We have identified the family of SGT genes expressed in the leaves of a medicinal plant Withania somnifera. One member (SGTL1) of this gene family was cloned. The full-length cDNA sequence of SGTL1 represents 2532 bp, comprising untranslated regions (UTRs) of 337 and 89 bp at the 5' and 3' ends, respectively. The amino acid sequence deduced from the 2103 bp open reading frame (ORF) showed homology (67-45%) to the reported plant SGTs. The presence of two putative transmembrane domains suggested the association of SGTL1 with membrane. The SGTL1 was expressed in Escherichia coli and recombinant enzyme from the supernatant was partially purified and biochemically characterized. The relative activity and kinetic properties of SGTL1 for different sterols were compared with a recombinant SGT (GenBank Accession No. Z83833) of Arabidopsis thaliana (AtSGT). Both the recombinant enzymes showed activity with 3-beta-OH sterols. The distribution of SGTL1 transcript in W. somnifera, as determined by quantitative PCR, showed higher expression in roots and mature leaves. Expression of the SGTL1 transcript in the leaves of W. somnifera was enhanced following the application of salicylic acid. In contrast, it decreased rapidly on exposure of the plants to heat shock, suggesting functional role of the enzyme in biotic and abiotic stresses. << Less
Arch Biochem Biophys 460:48-55(2007) [PubMed] [EuropePMC]
This publication is cited by 10 other entries.
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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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Purification and physico-kinetic characterization of 3beta-hydroxy specific sterol glucosyltransferase from Withania somnifera (L) and its stress response.
Madina B.R., Sharma L.K., Chaturvedi P., Sangwan R.S., Tuli R.
Sterol glycosyltransferases catalyze the synthesis of diverse glycosteroids in plants, leading to a change in their participation in cellular metabolism. Withania somnifera is a medically important plant, known for a variety of pharmacologically important withanolides and their glycosides. In this ... >> More
Sterol glycosyltransferases catalyze the synthesis of diverse glycosteroids in plants, leading to a change in their participation in cellular metabolism. Withania somnifera is a medically important plant, known for a variety of pharmacologically important withanolides and their glycosides. In this study, a cytosolic sterol glucosyltransferase was purified 3406 fold to near homogeneity from W. somnifera leaves and studied for its biochemical and kinetic properties. The purified enzyme was active with UDP-glucose but not with UDP-galactose as sugar donor. It exhibited broad sterol specificity by glucosylating a variety of sterols and phytosterols with 3beta-OH group. It showed a low level of activity with flavonoids and isoflavonoids. The enzyme gave maximum K(cat)/K(m) value (0.957) for 24-methylenecholesterol that resembles aglycone structure of pharmacologically important sitoindosides VII and VIII from W. somnifera. The enzyme follows ordered sequential bisubstrate mechanism of reaction, in which UDP-glucose and sterol are the first and second binding substrates. This is the first detailed kinetic study on purified plant cytosolic sterol glucosyltransferases. Results on peptide mass fingerprinting and substrate specificity suggested that the enzyme belongs to the family of secondary metabolite glucosylating glucosyltransferases. The enzyme activity exhibited a rapid in vivo response to high temperature and salicylic acid treatment of plants, suggesting its physiological role in abiotic and biotic stress. << Less
Biochim Biophys Acta 1774:392-402(2007) [PubMed] [EuropePMC]
This publication is cited by 9 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 (