“Cyanohydrin beta-glucosyltransferase”的意思、由来-开放百科全书

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Cyanohydrin beta-glucosyltransferase

释义

References

{{enzyme
| Name = cyanohydrin beta-glucosyltransferase
| EC_number = 2.4.1.85
| CAS_number = 55354-52-4
| IUBMB_EC_number = 2/4/1/85
| GO_code = 0047792
| image =
| width =
| caption =
}}

In enzymology, a cyanohydrin beta-glucosyltransferase ({{EC number|2.4.1.85}}) is an enzyme that catalyzes the chemical reaction

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

{{cite journal | vauthors = Reay PF, Conn EE |author-link2=Eric Conn | date = 1974 | title = The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin beta-glucosyltransferase from sorghum seedlings | journal = J. Biol. Chem. | volume = 249 | pages = 5826–30 | pmid = 4416442 | issue = 18 }}
{{cite journal | vauthors = Jones PR, Moller BL, Hoj PB | date = 1999 | title = 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 | journal = J. Biol. Chem. | volume = 274 | pages = 35483–91 | pmid = 10585420 | doi = 10.1074/jbc.274.50.35483 | issue = 50 }}
{{cite journal | author = Moller BL | date = 2003 | title = The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor | journal = Phytochemistry | volume = 64 | pages = 143–51 | pmid = 12946413 | doi = 10.1016/S0031-9422(03)00261-9 | last2 = Kristensen | first2 = C | last3 = Tattersall | first3 = DB | last4 = Jones | first4 = PR | last5 = Olsen | first5 = CE | last6 = Bak | first6 = S | last7 = Møller | first7 = BL | issue = 1 }}
{{cite journal | vauthors = Busk PK, Moller BL | date = 2002 | title = Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants | journal = Plant Physiol. | volume = 129 | pages = 1222–31 | pmid = 12114576 | doi = 10.1104/pp.000687 | issue = 3 | pmc = 166516 }}
{{cite journal | author = BL, Bak S | date = 2005 | title = Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | pages = 1779–84 | pmid = 15665094 | doi = 10.1073/pnas.0409233102 | last2 = Morant | first2 = M | last3 = Olsen | first3 = CE | last4 = Ekstrøm | first4 = CT | last5 = Galbraith | first5 = DW | last6 = Møller | first6 = BL | last7 = Bak | first7 = S | issue = 5 | pmc = 545087 }}

2 : EC 2.4.1|Enzymes of unknown structure

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