Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | UDPGT |
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