Literature summary for 3.2.2.27 extracted from

Xiao, G.; Tordova, M.; Jagadeesh, J.; Drohat, A.C.; Stivers, J.T.; Gilliland, G.L.
Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited (1999), Proteins, 35, 13-24.

Search for more literature for 3.2.2.27

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
strain B UDG free or in complex with uracil or glycerol, X-ray diffraction structure determination and analysis at 1.60, 1.50, and 1.43 A resolution, respectively	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D64N	site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme	Escherichia coli
H187Q	site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	steady-state kinetics of wild-type and mutant enzymes	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli B / ATCC 11303	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil	active site structure and catalytic mechanism, overview	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
uracil-mismatched double-stranded DNA + H2O	substrate specificity, overview	Escherichia coli	uracil + double-stranded DNA with abasic site	-	?
uracil-mismatched double-stranded DNA + H2O	substrate specificity, overview	Escherichia coli B / ATCC 11303	uracil + double-stranded DNA with abasic site	-	?

Subunits

Subunits	Comment	Organism
More	structure comparison to the human and Herpes simplex virus enzymes, overview	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Escherichia coli

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.3	10.4	-	Escherichia coli

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Release 2023.1 (January 2023)