Information on EC 3.1.12.1 - 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.12.1
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RECOMMENDED NAME
GeneOntology No.
5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
poly-dC10 + H2O
cytidine 3'-phosphate + ?
show the reaction diagram
single-stranded oligodeoxyribonucleotide + H2O
nucleoside 3'-phosphate + ?
show the reaction diagram
ssDNA + H2O
nucleoside 3'-phosphate + ?
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iron-sulfur centre
K+
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nuclease activity of the enzyme is maximal in the presence of 20-200 mM KCl
additional information
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Ca2+ does not support the nuclease activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23239
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x * 23239, calculated from sequence
170000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure reveals a decameric toroid with a large 55 A diameter central channel formed by five tightly packed dimers
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable
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4°C, enzyme loses colour and activity over several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Posetta DE3
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C188A
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the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
C191A
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the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
C32A
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the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
C188A
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the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
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C191A
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the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
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C32A
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the mutant protein is inactive in both binding and cleavage of ssDNA. It forms various protein aggregates
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D99A
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inactive mutant enzyme; the mutant enzyme fails to cut DNA
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