In enzymology, a cyanohydrin beta-glucosyltransferase (EC 2.4.1.85) is an enzyme that catalyzes the chemical reaction
| cyanohydrin beta-glucosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.85 | ||||||||
| CAS no. | 55354-52-4 | ||||||||
| 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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- UDP-D-glucose + (S)-4-hydroxymandelonitrile UDP + (S)-4-hydroxymandelonitrile beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-D-glucose and (S)-4-hydroxymandelonitrile, whereas its two products are UDP and (S)-4-hydroxymandelonitrile beta-D-glucoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-D-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-p-hydroxymandelonitrile, glucosyltransferase, UDP-glucose-p-hydroxymandelonitrile glucosyltransferase, uridine diphosphoglucose-cyanohydrin glucosyltransferase, uridine diphosphoglucose:aldehyde cyanohydrin, beta-glucosyltransferase, UDP-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase, UGT85B1, and UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase. This enzyme participates in tyrosine metabolism and cyanoamino acid metabolism.
References
edit- Reay PF, Conn EE (1974). "The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin beta-glucosyltransferase from sorghum seedlings". J. Biol. Chem. 249 (18): 5826–30. doi:10.1016/S0021-9258(20)79891-1. PMID 4416442.
- Jones PR, Moller BL, Hoj PB (1999). "The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity". J. Biol. Chem. 274 (50): 35483–91. doi:10.1074/jbc.274.50.35483. PMID 10585420.
- Moller BL; Kristensen, C; Tattersall, DB; Jones, PR; Olsen, CE; Bak, S; Møller, BL (2003). "The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor". Phytochemistry. 64 (1): 143–51. doi:10.1016/S0031-9422(03)00261-9. PMID 12946413.
- Busk PK, Moller BL (2002). "Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants". Plant Physiol. 129 (3): 1222–31. doi:10.1104/pp.000687. PMC 166516. PMID 12114576.
- BL, Bak S; Morant, M; Olsen, CE; Ekstrøm, CT; Galbraith, DW; Møller, BL; Bak, S (2005). "Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome". Proc. Natl. Acad. Sci. U.S.A. 102 (5): 1779–84. doi:10.1073/pnas.0409233102. PMC 545087. PMID 15665094.
