Information on EC 2.4.1.26 - DNA alpha-glucosyltransferase

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The expected taxonomic range for this enzyme is: Enterobacteria phage T4 sensu lato

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EC NUMBER
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2.4.1.26
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RECOMMENDED NAME
GeneOntology No.
DNA alpha-glucosyltransferase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
Transfers an alpha-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
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LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:DNA alpha-D-glucosyltransferase
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CAS REGISTRY NUMBER
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9030-13-1
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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli infected with
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Manually annotated by BRENDA team
Escherichia coli infected with
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + hydroxymethylated DNA
UDP + glycosylated hydroxymethylated DNA
show the reaction diagram
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Glu22 seems not to be responsible for activation of the nucleophilic attack, Ser106 and Glu311 probably form a salt bridge in the closed enzyme formation, Glu311 is probably involved in interaction with UDP-glucose, Arg236, Arg256 and Met231 are probably involved in interaction with the DNA
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?
UDPglucose + 5-hydroxymethylcytosine containing DNA
UDP + alpha-glucosyl-5-hydroxymethylcytosine containing DNA
show the reaction diagram
additional information
?
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hydroxymethylated DNA binding activities of wild-type and mutant enzymes, the enzyme undergoes a conformational change from a substrate-free open form to a closed substrate-binding form stabilized by several salt bridges and probably involving Ser106 and Glu22
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METALS and IONS
ORGANISM
UNIPROT
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LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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LITERATURE
IMAGE
Phosphate buffer
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stimulates
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sulfhydryl reagents
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required
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
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LITERATURE
46651
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x * 46651, Escherichia coli infected with bacteriophageT4, calculation from nucleotide sequence
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SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
?
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x * 46651, Escherichia coli infected with bacteriophageT4, calculation from nucleotide sequence
additional information
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secondary structure alignment
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, E. coli infected with
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain XL1 by metal affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene agt, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL1
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ENGINEERING
ORGANISM
UNIPROT
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LITERATURE
E22A
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site-directed mutagenesis, 50% activity compared to the wild-type enzyme, in absence of acceptor 70% reduced UDG-glucose turnover compared to the wild-type enzyme
E311A
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site-directed mutagenesis, 1-2% activity compared to the wild-type enzyme, in absence of acceptor no remaining UDG-glucose turnover
M231A
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site-directed mutagenesis, 1-2% activity compared to the wild-type enzyme, in absence of acceptor mutant shows an unaltered UDG-glucose turnover compared to the wild-type enzyme
R236A
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site-directed mutagenesis, 27% activity compared to the wild-type enzyme, in absence of acceptor mutant shows an unaltered UDG-glucose turnover compared to the wild-type enzyme
R256A
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site-directed mutagenesis, activity is similar to the wild-type enzyme, in absence of acceptor mutant shows an unaltered UDG-glucose turnover compared to the wild-type enzyme
S106A
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site-directed mutagenesis, 111% activity compared to the wild-type enzyme, in absence of acceptor mutant shows an unaltered UDG-glucose turnover compared to the wild-type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.26)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)