Cyanohydrin beta-glucosyltransferase
| Cyanohydrin beta-glucosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.85 | ||||||||
| CAS no. | 55354-52-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Cyanohydrin beta-glucosyltransferase (EC 2.4.1.85) is an enzyme that catalyzes the chemical reaction:[1]
-4-hydroxymandelonitrile.svg.png)
Tyrosine N-monooxygenase, the first enzyme in the pathway to dhurrin, converts L-tyrosine to (E)-(4-hydroxyphenyl)acetaldehyde oxime. Subsequently, (S)-4-hydroxymandelonitrile is formed by the action of 4-hydroxyphenylacetaldehyde oxime monooxygenase.[2]
Cyanohydrin beta-glucosyltransferase uses uridine diphosphate glucose (UDP-D-glucose) to add the glucoside component.[3][4] The enzyme is a glycosyltransferase, specifically one of 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.[5]
The enzyme from Sorghum bicolor can act on a range of alcohols, not just the cyanohydrin group of 4-hydroxymandelonitrile.[6]
References
- ↑ 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.
- ↑ Clausen, Mette; Kannangara, Rubini M.; Olsen, Carl E.; et al. (2015). "The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways". The Plant Journal. 84 (3): 558–573. doi:10.1111/tpj.13023. PMID 26361733.
- ↑ Busk, Peter Kamp; Møller, Birger Lindberg (2002). "Dhurrin Synthesis in Sorghum is Regulated at the Transcriptional Level and Induced by Nitrogen Fertilization in Older Plants". Plant Physiology. 129 (3): 1222–1231. doi:10.1104/pp.000687. PMC 166516. PMID 12114576.
- ↑ Kristensen, Charlotte; Morant, Marc; Olsen, Carl Erik; Ekstrøm, Claus T.; Galbraith, David W.; Lindberg Møller, Birger; Bak, Søren (2005). "Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome". Proceedings of the National Academy of Sciences. 102 (5): 1779–1784. doi:10.1073/pnas.0409233102. PMC 545087. PMID 15665094.
- ↑ Enzyme 2.4.1.85 at KEGG Pathway Database.
- ↑ Hansen, Karina Sinding; Kristensen, Charlotte; Tattersall, David Bruce; Jones, Patrik Raymond; Olsen, Carl Erik; Bak, Søren; Møller, Birger Lindberg (2003). "The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor". Phytochemistry. 64 (1): 143–151. doi:10.1016/S0031-9422(03)00261-9. PMID 12946413.
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