Alizarin 2-beta-glucosyltransferase
alizarin 2-beta-glucosyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 2.4.1.103 | ||||||||
CAS number | 74506-41-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
|
In enzymology, an alizarin 2-beta-glucosyltransferase (EC 2.4.1.103) is an enzyme that catalyzes the chemical reaction
- UDP-glucose + alizarin UDP + 1-hydroxy-2-(beta-D-glucosyloxy)-9,10-anthraquinone
Thus, the two substrates of this enzyme are UDP-glucose and alizarin, whereas its two products are UDP and 1-hydroxy-2-(beta-D-glucosyloxy)-9,10-anthraquinone.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:1,2-dihydroxy-9,10-anthraquinone 2-O-beta-D-glucosyltransferase. This enzyme is also called uridine diphosphoglucose-alizarin glucosyltransferase.
References
- Mateju J, Cudlin J, Steinerova N, Blumauerova M, Vanek Z (1979). "Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens". Folia. Microbiol. (3): 205–10. PMID 38193.
This article is issued from Wikipedia - version of the 11/9/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.