N-hydroxythioamide S-beta-glucosyltransferase
thiohydroximate beta-D-glucosyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.1.195 | ||||||||
CAS no. | 9068-14-8 | ||||||||
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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In enzymology, a N-hydroxythioamide S-beta-glucosyltransferase (EC 2.4.1.195) is an enzyme that catalyzes the chemical reaction
- UDP-glucose + N-hydroxy-2-phenylethanethioamide UDP + desulfoglucotropeolin
Thus, the two substrates of this enzyme are UDP-glucose and N-hydroxy-2-phenylethanethioamide, whereas its two products are UDP and desulfoglucotropeolin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:N-hydroxy-2-phenylethanethioamide S-beta-D-glucosyltransferase. Other names in common use include desulfoglucosinolate-uridine diphosphate glucosyltransferase, uridine diphosphoglucose-thiohydroximate glucosyltransferase, thiohydroximate beta-D-glucosyltransferase, UDPG:thiohydroximate glucosyltransferase, thiohydroximate S-glucosyltransferase, thiohydroximate glucosyltransferase, and UDP-glucose:thiohydroximate S-beta-D-glucosyltransferase.
References
[edit]- Jain JC, Reed DW, GrootWassink JW, Underhill EW (1989). "A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species". Anal. Biochem. 178 (1): 137–40. doi:10.1016/0003-2697(89)90369-2. PMID 2524977.
- Reed DW, Davin L, Jain JC, Deluca V, Nelson L, Underhill EW (1993). "Purification and properties of UDP-glucose:thiohydroximate glucosyltransferase from Brassica napus L. seedlings". Arch. Biochem. Biophys. 305 (2): 526–32. doi:10.1006/abbi.1993.1456. PMID 8373190.
- Fahey JW, Zalcmann AT, Talalay P (2001). "The chemical diversity and distribution of glucosinolates and isothiocyanates among plants". Phytochemistry. 56 (1): 5–51. doi:10.1016/S0031-9422(00)00316-2. PMID 11198818.
- TF; Abel S (2004). "Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate biosynthesis and auxin homeostasis". Plant J. 40 (6): 893–908. CiteSeerX 10.1.1.538.667. doi:10.1111/j.1365-313X.2004.02261.x. PMID 15584955.