Reaction participants Show >> << Hide
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline wogonin 7-O-β-D-glucuronate Identifier CHEBI:61285 Charge -1 Formula C22H19O11 InChIKeyhelp_outline LNOHXHDWGCMVCO-NTKSAMNMSA-M SMILEShelp_outline COc1c(O[C@@H]2O[C@@H]([C@@H](O)[C@H](O)[C@H]2O)C([O-])=O)cc(O)c2c1oc(cc2=O)-c1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-glucuronate Identifier CHEBI:58720 (Beilstein: 4189951) help_outline Charge -1 Formula C6H9O7 InChIKeyhelp_outline AEMOLEFTQBMNLQ-AQKNRBDQSA-M SMILEShelp_outline OC1O[C@@H]([C@@H](O)[C@H](O)[C@H]1O)C([O-])=O 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 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline wogonin Identifier CHEBI:78338 Charge -1 Formula C16H11O5 InChIKeyhelp_outline XLTFNNCXVBYBSX-UHFFFAOYSA-M SMILEShelp_outline COc1c([O-])cc(O)c2c1oc(cc2=O)-c1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:28326 | RHEA:28327 | RHEA:28328 | RHEA:28329 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Purification and properties of a plant beta-D-glucuronidase form Scutellaria root.
Ikegami F., Matsunae K., Hisamitsu M., Kurihara T., Yamamoto T., Murakoshi I.
beta-D-Glucuronidase (baicalinase, GUS [EC 3.2.1.31]) activity in the crude drug, Scutellaria root, was assayed in line with the quality control standards of Kampo (Japanese Herbal) medicines. GUS was purified to homogeneity in the purification steps including DEAE-Sepharose Fast Flow and chromato ... >> More
beta-D-Glucuronidase (baicalinase, GUS [EC 3.2.1.31]) activity in the crude drug, Scutellaria root, was assayed in line with the quality control standards of Kampo (Japanese Herbal) medicines. GUS was purified to homogeneity in the purification steps including DEAE-Sepharose Fast Flow and chromatofocusing used PBETM94 and Polybuffer 74. These results suggest that the Scutellaria GUS is composed of 55kDa active subunits and that the isoelectric point of this enzyme is pH 5.4. Optimal catalytic activity was found at pH 4.7 in the pH range 3.6--6.2 in 50 mM Na-citrate buffer. The purified enzyme hydrolyzed baicalin and wogonin glucuronide, but did not hydrolyze glycyrrhizin or some beta-glucosides found in other crude drugs. GUS activity in several crude drugs is also described. << Less
Biol. Pharm. Bull. 18:1531-1534(1995) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Molecular characterization of a novel beta-glucuronidase from Scutellaria baicalensis georgi.
Sasaki K., Taura F., Shoyama Y., Morimoto S.
We cloned a gene encoding Scutellaria beta-glucuronidase (sGUS) that is involved in the initiation of H(2)O(2) metabolism in skullcap (Scutellaria baicalensis). This gene consists of a 1581-nucleotide open reading frame, the deduced amino acid sequence of which contains an ATP/GTP binding site and ... >> More
We cloned a gene encoding Scutellaria beta-glucuronidase (sGUS) that is involved in the initiation of H(2)O(2) metabolism in skullcap (Scutellaria baicalensis). This gene consists of a 1581-nucleotide open reading frame, the deduced amino acid sequence of which contains an ATP/GTP binding site and a leucine zipper motif. sGUS has apparent similarity to the heparan sulfate-metabolizing beta-glucuronidase heparanase but no homology to family 2 beta-glucuronidases. In addition, neither the family 2 glycosylhydrolase signature nor family 2 acid-base catalyst was found in this enzyme. These results suggested that sGUS does not belong to the family 2 beta-glucuronidases. We modified several residues predicted to act as the acid-base or nucleophilic residue of sGUS by site-directed mutagenesis. Mutations at Glu(212) or Glu(329) resulted in much lower k(cat)/K(m) values in the mutants as compared with the wild-type enzyme, indicating that these are the acid-base and nucleophilic residues of the active site, respectively. Moreover, similar site-directed mutagenesis confirmed that Tyr(281) is also involved in the beta-glucuronidase activity. The amino acid sequences of small regions containing these active site residues were conserved in heparanases. As sGUS has various structural characteristics in common with heparanase, we concluded that sGUS and heparanase belong to the same new family. << Less
J. Biol. Chem. 275:27466-27472(2000) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.