Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT) is involved in the modification of grape anthocyanins and thus could affect their color stability. The color plays a significant role in the in agricultural produce, such as table grapes and wine.

Introduction

Vv3GT belongs to Glycosyltransferases (GTs), a large family of enzymes involved in the transfer of sugar residues from a sugar donor to various substrates. Glycosylation of metabolites in plants is usually catalyzed by glycosyltransferases (GTs) belonging to the GT1 sub-family (as classified by the CAZy database [1], which use UDP-activated sugars as the major donor molecule and are thus referred to as UGTs.

Disease

Relevance

Structural highlights

Despite low primary sequence similarity, the secondary and tertiary structures of GTs are highly conserved. ^[1]

Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.

Vv3GT with the two Rossmann-like domains colored in pink

The plant UGTs are characterized by sharing a highly conserved motif referred to as the PSPG motif (Plant Secondary Product Glycosyltransferase motif).

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