| DOI | Resolve DOI: https://doi.org/10.1006/abbi.1993.1456 |
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| Author | Search for: Reed, D.W.1; Search for: Davin, L.1; Search for: Jain, J.C.1; Search for: Deluca, V.1; Search for: Nelson, L.1; Search for: Underhill, E.W.1 |
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| Affiliation | - National Research Council of Canada. NRC Plant Biotechnology Institute
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| Format | Text, Article |
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| Subject | UDP-Glucose; Brassica napus; purification |
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| Abstract | A uridinediphosphateglucose:thiohydroximate glucosyltransferase (EC 2.4.1.-) has been purified 3700-fold from Brassica napus L. seedlings. The enzyme catalyzes the formation of desulfoglucosinolates by transfer of glucose from UDP-glucose to thiohydroximates and is believed to be the second to last step involved in glucosinolate biosynthesis. The enzyme was purified to near homogeneity, exhibiting a single band by non-denaturing polyacrylamide gel electrophoresis (PAGE) and on sodium dodecyl sulfate-PAGE (Mr 46,000) but showed multiple isoforms between pH 4.6 and 4.3 when resolved by IEF. The enzyme is stable at temperatures up to 30°C for at least 1 h and shows maximum activity rates at pH 6.0 and has no absolute requirements for cations. The Km values for UDP-glucose and phenylacetothiohydroximate were calculated to be 0.46 and 0.05 mM, respectively. This enzyme possesses a high degree of specificity for the thiohydroximic functional group but little specificity for the associated side-chain groups. Similar enzyme activity has been detected in all other members of the Brassicaceae family tested and is believed to be a common thiohydroximate glucosylating enzyme present in these and other glucosinolate producing plants. |
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| Publication date | 1993 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRCC 36488 |
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| NPARC number | 21275383 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 8b52391e-c718-40dc-bf15-e6d2bb2d3fbb |
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| Record created | 2015-06-24 |
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| Record modified | 2020-04-24 |
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