T4-phage β−glucosyltransferase, also known as UDP glucose-DNA β-glucosyltransferase, (Genbank Accession No. NP_049658) amino acids 1-351(end) with C-terminal His-tag, MW= 41.6 kDa, expressed in Escherichia coli.
Application
Useful for the differentiation of hydroxymethylcytosine (HMC) from methylcytosine in DNA, via glucosylating HMC and protecting HMC from endonuclease cleavage.
Biochem/physiol Actions
T4-phage β-glucosyltransferase is involved in the transfer of glucose from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA of the T4-phage. Ions such as Mg2+, Mn2+ and Ca2+ activate this enzyme.[1][2][3]
In contrast to 5-methylcytosine (5-mC), which has been studied extensively, little is known about 5-hydroxymethylcytosine (5-hmC), a recently identified epigenetic modification present in substantial amounts in certain mammalian cell types. Here we present a method for determining the genome-wide distribution
High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding.
Morera S
Journal of Molecular Biology, 311(3), 569-577 (2001)
The resistance of Escherichia coli O157:H7 to disinfection is associated with its ability to form biofilms, mainly constituted by glucans produced by glucosyltransferases. Citral and geraniol, terpenes found in the essential oil of Cymbopogon citratus (EO), have proven antibacterial activity
T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism.
Morera S
Journal of Molecular Biology, 292(3), 717-730 (1999)
Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.
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