Literature summary for 3.1.21.1 extracted from

Ho, T.Y.; Wu, S.L.; Hsiang, C.H.; Chang, T.J.; Hsiang, C.Y.
Identification of a DNA-binding domain and an active-site residue of pseudorabies virus DNase (2000), Biochem. J., 346, 441-445.

No PubMed abstract available

Search for more literature for 3.1.21.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and deletion mutants in Escherichia coli BL21 (DE3)	Suid alphaherpesvirus 1

Protein Variants

Protein Variants	Comment	Organism
H371A	site-directed mutagenesis, exchange of a well-conserved His residue, loss of most of the nuclease activity, stilla ctive in DNA-binding	Suid alphaherpesvirus 1
additional information	construction of mutants with deletions at the N- and/or the C-terminus, mutants reveal the localisation fo activities within the enzyme sequence, overview	Suid alphaherpesvirus 1

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Suid alphaherpesvirus 1

Organism

Organism	UniProt	Comment	Textmining
Suid alphaherpesvirus 1	-	i.e. PRV	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and deletion mutants from Escherichia coli, to homogeneity	Suid alphaherpesvirus 1

Reaction

Reaction	Comment	Organism	Reaction ID
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products	catalytic mechanism, the N-terminal 62 residues and the C-terminal 39 residues have important roles in 3'-exonuclease activity, residues 63-453 are responsible for 5'- and 3'-exonuclease activities, residues 24-492 form a region with 7fold higher catalytic activity than the intact enzyme	Suid alphaherpesvirus 1	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	5'-exonuclease, 3'-exonuclease and DNA-binding activities of wild-type and truncated mutants and mutant H371A	Suid alphaherpesvirus 1

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pUC18 DNA + H2O	-	Suid alphaherpesvirus 1	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme is divided into a catalytic domain and a DNA-binding domain	Suid alphaherpesvirus 1

Synonyms

Synonyms	Comment	Organism
alkaline nuclease	-	Suid alphaherpesvirus 1
DNase	-	Suid alphaherpesvirus 1

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Suid alphaherpesvirus 1

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9	-	assay at	Suid alphaherpesvirus 1

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Release 2023.1 (January 2023)