PS00375

UDP-glycosyltransferases signature

PROSITE patterns entry
Member databasePROSITE patterns
PROSITE patterns typeconserved site
Short nameUDPGT

Description

UDP glycosyltransferases (UGT) are a superfamily of enzymes that catalyzes the addition of the glycosyl group from a UTP-sugar to a small hydrophobic molecule. This family currently consist of: - Mammalian UDP-glucoronosyl transferases (EC 2.4.1.17) (UDPGT) [1,2]. A large family of membrane-bound microsomal enzymes which catalyze the transfer of glucuronic acid to a wide variety of exogenous and endogenous lipophilic substrates. These enzymes are of major importance in the detoxification and subsequent elimination of xenobiotics such as drugs and carcinogens. - A large number of putative UDPGT from Caenorhabditis elegans. - Mammalian 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
[1]
(EC 2.4.1.45) (also known as UDP-galactose-ceramide galactosyltransferase). This enzyme catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. - Plants flavonol O(3)-glucosyltransferase (EC 2.4.1.91). An enzyme [4] that catalyzes the transfer of glucose from UDP-glucose to a flavanol. This reaction is essential and one of the last steps in anthocyanin pigment biosynthesis. - Plants limonoid glucosyltransferase (EC 2.4.1.210). - Baculoviruses ecdysteroid UDP-glucosyltransferase (EC 2.4.1.-) [5] (egt). This enzyme catalyzes the transfer of glucose from UDP-glucose to ectysteroids which are insect molting hormones. The expression of egt in the insect host interferes with the normal insect development by blocking the molting process. - Prokaryotic zeaxanthin glucosyl transferase (EC 2.4.1.-) (gene crtX), an enzyme involved in carotenoid biosynthesis and that catalyses the glycosylation reaction which converts zeaxanthin to zeaxanthin-beta- diglucoside. - Streptomyces macrolide glycosyltransferases (EC 2.4.1.-)
[2]
. These enzymes specifically inactivates macrolide anitibiotics via 2'-O-glycosylation using UDP-glucose. These enzymes share a conserved domain of about 50 amino acid residues located in their C-terminal section and from which a pattern has been extracted to detect them.

References

1.Ceramide UDPgalactosyltransferase from myelinating rat brain: purification, cloning, and expression. Schulte S, Stoffel W. Proc. Natl. Acad. Sci. U.S.A. 90, 10265-9, (1993). View articlePMID: 7694285

2.Characterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation. Hernandez C, Olano C, Mendez C, Salas JA. Gene 134, 139-40, (1993). View articlePMID: 8244027

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