Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline 3'-phosphoadenylyl sulfate Identifier CHEBI:58339 Charge -4 Formula C10H11N5O13P2S InChIKeyhelp_outline GACDQMDRPRGCTN-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OS([O-])(=O)=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 106 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline quercetin Identifier CHEBI:57694 Charge -1 Formula C15H9O7 InChIKeyhelp_outline REFJWTPEDVJJIY-UHFFFAOYSA-M SMILEShelp_outline Oc1ccc(cc1O)-c1oc2cc([O-])cc(O)c2c(=O)c1O 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline adenosine 3',5'-bisphosphate Identifier CHEBI:58343 Charge -4 Formula C10H11N5O10P2 InChIKeyhelp_outline WHTCPDAXWFLDIH-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 140 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline quercetin 3-sulfate Identifier CHEBI:58254 Charge -2 Formula C15H8O10S InChIKeyhelp_outline DNAYVNOVGHZZLH-UHFFFAOYSA-L SMILEShelp_outline Oc1ccc(cc1O)-c1oc2cc([O-])cc(O)c2c(=O)c1OS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13453 | RHEA:13454 | RHEA:13455 | RHEA:13456 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Partial purification and characterization of three flavonol-specific sulfotransferases from Flaveria chloraefolia.
Varin L., Ibrahim R.K.
Three distinct flavonol-specific sulfotransferases were partially purified from the shoot tips of Flaveria chloraefolia A. Gray by fractional precipitation with ammonium sulfate, followed by gel filtration on Sephacryl S-200, 3'-phosphoadenosine 5-phosphate-Agarose affinity chromatography and chro ... >> More
Three distinct flavonol-specific sulfotransferases were partially purified from the shoot tips of Flaveria chloraefolia A. Gray by fractional precipitation with ammonium sulfate, followed by gel filtration on Sephacryl S-200, 3'-phosphoadenosine 5-phosphate-Agarose affinity chromatography and chromatofocusing on Mono P. These enzymes exhibited expressed specificity for positions 3 of various flavonol acceptors and of 3' and 4' of flavonol 3-sulfate. The three sulfotransferases had similar molecular weights (35,000), exhibited no requirement for divalent cations and were not inhibited by SH group reagents. Their K(m) values for both the sulfate donor and the flavonol acceptors were of the same order of magnitude (ca. 0.2-0.4 micromolar). Except for the 3-sulfotransferase, which exhibited two optima at pH 6.5 and 8.5, the 3' and the 4'-sulfotransferases had a pH optimum of 7.5. The three enzymes could be resolved only by chromatofocusing and were eluted at pH 5.4, pH 6.0, and pH 5.1 for the 3-, 3'- and 4'-sulfotransferases, respectively. The substrate specificity of these three enzymes is discussed in relation to the biosynthesis of polysulfated flavonols in F. chloraefolia. << Less
Plant Physiol. 90:977-981(1989) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Recent developments in the study of the structure-function relationship of flavonol sulfotransferases.
Marsolais F., Varin L.
With the rapid proliferation of sulfotransferase (ST) cDNA sequences in the last 5 years, consensus sequences were identified in four conserved regions. The association of these regions with substrate binding or catalysis was tested in several site-directed mutagenesis studies. Due to their strict ... >> More
With the rapid proliferation of sulfotransferase (ST) cDNA sequences in the last 5 years, consensus sequences were identified in four conserved regions. The association of these regions with substrate binding or catalysis was tested in several site-directed mutagenesis studies. Due to their strict substrate and position specificities, the flavonol 3- and 4'-STs represent an advantageous model system for the study of the structure-function relationship of cytosolic STs. Using a combination of chimeric and site-directed mutant proteins, a domain was identified containing all the determinants responsible for the substrate specificity of these enzymes, and characterized amino acid residues conserved in all cloned STs that are involved in substrate binding and catalysis. This paper summarizes the results of these studies. << Less
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Novel flavonol 3-sulfotransferase. Purification, kinetic properties, and partial amino acid sequence.
Varin L., Ibrahim R.K.
A flavonol sulfotransferase (EC 2.8.2.-), which catalyzes the transfer of the sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the 3-hydroxyl group of flavonol aglycones, has been purified to apparent homogeneity from Flaveria chloraefolia. The specific activity of flavonol 3-sulfotrans ... >> More
A flavonol sulfotransferase (EC 2.8.2.-), which catalyzes the transfer of the sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the 3-hydroxyl group of flavonol aglycones, has been purified to apparent homogeneity from Flaveria chloraefolia. The specific activity of flavonol 3-sulfotransferase was enriched 2000-fold, as compared with the homogenate, with a recovery of 9%. The molecular mass of the native and denatured enzyme was found to be 34.5 kDa, suggesting that the active from of the enzyme is a monomer. The enzyme exhibited expressed specificity for position 3 of flavonol aglycones, showed two activity optima at pH 6.0 and 8.5, did not require divalent cations, and was not inhibited by either EDTA or sulfhydryl group reagents. The results of substrate interaction kinetics and product inhibition are consistent with an Ordered Bi Bi mechanism where 3'-phosphoadenosine 5'-phosphosulfate is the first substrate to bind to the enzyme and 3'-phosphoadenosine 5'-phosphate is the final product to be released. The amino acid sequence of two peptides representing 17 and 33 amino acids showed no significant sequence similarity with the amino acid sequences reported for animal sulfotransferases. Antibodies raised against F. chloraefolia 3-sulfotransferase were found to cross-react with the 3'- and 4'-sulfotransferase activities of the same plant, suggesting that the three enzymes are structurally related. << Less