Difference between revisions of "Part:BBa K4395009"
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| + | VvGT2 was originally identified in Vitis vinifera. It is one of the hydroxybenzoic acid / hydroxycinnamic acid Glucosyltransferases co-expressed with genes related to proanthocyanidin biosynthesis. It is mainly expressed in pulp, which would fit with an involvement in the hydroxycinnamate pathway. It is also known as Vv galloyl glucosyl transferase 2 (VvgGT 2) because it can form glucose esters with a variety of phenolic acids, especially gallic acid. Substrate specificity studies showed that Vvgt2 could recognize a variety of substrates, including hydroxybenzoic acid and hydroxycinnamic acid, showing a slight preference for hydroxycinnamic acid. At the same time, VvGT2 exhibited a strict regio-specificity for the acceptor site, being able to glycosylate substrates by attaching the glucose to their carboxyl group. The maximal glucosyltransferase activity was observed at 6.5 for VvGT2 and this activity decreased at higher pH[1]. | ||
| + | Considering that Vvgt2 is capable of transferring the glucose residues regio- and stereoselectively from the activated sugar donor UDP-glucose(UDP-Glc) to hydroxybenzoic acid / hydroxycinnamic acid, it has been used to develop an in vivo glucosylation platform coupled with production and growth, and successfully realized the glycosylation of a series of small molecules in Escherichia coli W. Expression of vvGT2 enabled the strain to efficiently produce 14 glucose esters of various hydroxycinnamates and hydroxybenzoates with conversion yields up to 100%[2]. | ||
| + | References:[1] Khater F, Fournand D, Vialet S, Meudec E, Cheynier V, Terrier N. Identification and functional characterization of cDNAs coding for hydroxybenzoate/hydroxycinnamate glucosyltransferases co-expressed with genes related to proanthocyanidin biosynthesis. J EXP BOT 2012, 63(3): 1201-1214.[2] De Bruyn F, De Paepe B, Maertens J, Beauprez J, De Cocker P, Mincke S, Stevens C, De Mey M. Development of an in vivo glucosylation platform by coupling production to growth: Production of phenolic glucosides by a glycosyltransferase of Vitis vinifera. BIOTECHNOL BIOENG 2015, 112(8): 1594-1603. | ||
Latest revision as of 07:18, 4 October 2022
VvGT2 was originally identified in Vitis vinifera. It is one of the hydroxybenzoic acid / hydroxycinnamic acid Glucosyltransferases co-expressed with genes related to proanthocyanidin biosynthesis. It is mainly expressed in pulp, which would fit with an involvement in the hydroxycinnamate pathway. It is also known as Vv galloyl glucosyl transferase 2 (VvgGT 2) because it can form glucose esters with a variety of phenolic acids, especially gallic acid. Substrate specificity studies showed that Vvgt2 could recognize a variety of substrates, including hydroxybenzoic acid and hydroxycinnamic acid, showing a slight preference for hydroxycinnamic acid. At the same time, VvGT2 exhibited a strict regio-specificity for the acceptor site, being able to glycosylate substrates by attaching the glucose to their carboxyl group. The maximal glucosyltransferase activity was observed at 6.5 for VvGT2 and this activity decreased at higher pH[1]. Considering that Vvgt2 is capable of transferring the glucose residues regio- and stereoselectively from the activated sugar donor UDP-glucose(UDP-Glc) to hydroxybenzoic acid / hydroxycinnamic acid, it has been used to develop an in vivo glucosylation platform coupled with production and growth, and successfully realized the glycosylation of a series of small molecules in Escherichia coli W. Expression of vvGT2 enabled the strain to efficiently produce 14 glucose esters of various hydroxycinnamates and hydroxybenzoates with conversion yields up to 100%[2].
References:[1] Khater F, Fournand D, Vialet S, Meudec E, Cheynier V, Terrier N. Identification and functional characterization of cDNAs coding for hydroxybenzoate/hydroxycinnamate glucosyltransferases co-expressed with genes related to proanthocyanidin biosynthesis. J EXP BOT 2012, 63(3): 1201-1214.[2] De Bruyn F, De Paepe B, Maertens J, Beauprez J, De Cocker P, Mincke S, Stevens C, De Mey M. Development of an in vivo glucosylation platform by coupling production to growth: Production of phenolic glucosides by a glycosyltransferase of Vitis vinifera. BIOTECHNOL BIOENG 2015, 112(8): 1594-1603.