KEGG   ENZYME: 3.2.1.167
Entry
EC 3.2.1.167                Enzyme                                 
Name
baicalin-beta-D-glucuronidase;
baicalinase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Sysname
5,6,7-trihydroxyflavone-7-O-beta-D-glucupyranosiduronate glucuronosylhydrolase
Reaction(IUBMB)
baicalin + H2O = baicalein + D-glucuronate [RN:R09533]
Reaction(KEGG)
R09533
Substrate
baicalin [CPD:C10025];
H2O [CPD:C00001]
Product
baicalein [CPD:C10023];
D-glucuronate [CPD:C00191]
Comment
The enzyme also hydrolyses wogonin 7-O-beta-D-glucuronide and oroxylin 7-O-beta-D-glucuronide with lower efficiency [4]. Neglegible activity with p-nitrophenyl-beta-D-glucuronide [2].
History
EC 3.2.1.167 created 2011
Orthology
K20833  baicalin-beta-D-glucuronidase
Reference
1  [PMID:8593473]
  Authors
Ikegami F, Matsunae K, Hisamitsu M, Kurihara T, Yamamoto T, Murakoshi I
  Title
Purification and properties of a plant beta-D-glucuronidase form Scutellaria root.
  Journal
Biol Pharm Bull 18:1531-4 (1995)
DOI:10.1248/bpb.18.1531
  Sequence
Reference
2
  Authors
Zhang, C., Zhang, Y., Chen, J. and Liang, X.
  Title
Purification and characterization of baicalin-beta-D-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge.
  Journal
Proc Biochem 40:1911-1915 (2005)
Reference
3  [PMID:10858442]
  Authors
Sasaki K, Taura F, Shoyama Y, Morimoto S
  Title
Molecular characterization of a novel beta-glucuronidase from Scutellaria baicalensis georgi.
  Journal
J Biol Chem 275:27466-72 (2000)
DOI:10.1074/jbc.M004674200
  Sequence
Reference
4
  Authors
Morimoto, S., Harioka, T. and Shoyama, Y.
  Title
Purification and characterization of flavone-specific beta-glucuronidase from callus cultures of Scutellaria baicalensis Georgi.
  Journal
Planta 195:535-540 (1995)
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.167
IUBMB Enzyme Nomenclature: 3.2.1.167
ExPASy - ENZYME nomenclature database: 3.2.1.167
BRENDA, the Enzyme Database: 3.2.1.167

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