Amygdalin beta-glucosidase
| amygdalin β-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.117 | ||||||||
| CAS no. | 51683-43-3 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme amygdalin β-glucosidase (EC 3.2.1.117) catalyzes the following chemical reaction:
Thus, the two substrates of this enzyme are (R)-amygdalin and H2O, whereas its two products are (R)-prunasin and D-glucose.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is amygdalin beta-D-glucohydrolase. Other names in common use include amygdalase, amygdalinase, amygdalin hydrolase, and amygdalin glucosidase.
It can be completely inhibited by the action of Glucono-δ-lactone at 1 mM concentration.[1]
References
[edit]- ^ Petruccioli, M.; Brimer, L.; Cicalini, A. R.; et al. (1999). "Production and Properties of the Linamarase and Amygdalase Activities of Penicillium aurantiogriseum P35". Bioscience, Biotechnology, and Biochemistry. 63 (5): 805–812. doi:10.1271/bbb.63.805. PMID 10380623.
- Kuroki G, Lizotte PA, Poulton JE (1984). "Catabolism of (R)-Amygdalin and (R)-Vicianin by Partially Purified β-Glycosidases from Prunus serotina Ehrh. and Davallia trichomanoides". Z. Naturforsch. C. 39: 232–239.
