Biology:Beta-glucogallin—tetrakisgalloylglucose O-galloyltransferase
| Beta-glucogallin-tetrakisgalloylglucose O-galloyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.143 | ||||||||
| CAS number | 122653-70-7 | ||||||||
| 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 / QuickGO | ||||||||
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Beta-glucogallin-tetrakisgalloylglucose O-galloyltransferase (EC 2.3.1.143) is an enzyme that catalyzes the chemical reaction which transfers the fifth and final gallic acid unit to a central glucose molecule to form the gallotannin, pentagalloylglucose.
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme characterised from oak (Quercus robur) are glucogallin and 1,2,3,6-tetrakis-O-galloyl-β-D-glucose. Its products are D-glucose and pentagalloylglucose.[1] Gallotannins are widely found in foodstuffs.[2]
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1-O-galloyl-beta-D-glucose:1,2,3,6-tetrakis-O-galloyl-β-D-glucose 4-O-galloyltransferase. Other names in common use include β-glucogallin-tetragalloylglucose 4-galloyltransferase, β-glucogallin:1,2,3,6-tetra-O-galloylglucose, 4-O-galloyltransferase, β-glucogallin:1,2,3,6-tetra-O-galloyl-beta-D-glucose, and 4-O-galloyltransferase.[3]
References
- ↑ "Biosynthesis of gallotannins: beta-glucogallin-dependent formation of 1,2,3,4,6-pentagalloylglucose by enzymatic galloylation of 1,2,3,6-tetragalloylglucose". Arch. Biochem. Biophys. 273 (1): 58–63. 1989. doi:10.1016/0003-9861(89)90161-6. PMID 2757399.
- ↑ He, Hua-Feng (2022). "Recognition of Gallotannins and the Physiological Activities: From Chemical View". Frontiers in Nutrition 9. doi:10.3389/fnut.2022.888892. PMID 35719149.
- ↑ Enzyme 2.3.1.143 at KEGG Pathway Database.
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