3.1.12.1: 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
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For detailed information about 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming), go to the full flat file.
Reaction
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates =
Synonyms
5' to 3' single stranded DNA exonuclease, BH0340, Cas4, Cas4 nuclease, Cas4-1, Cas4-2, casC, CRISPR adaptation factor, CRISPR-associated Cas4 nuclease, CRISPR-associated exonuclease Cas4, CRISPR-associated protein 4, DUF83Pc, DUF83Ss, Pcal_0546, PF1119, PF1793, SSO0001, TTV1 nucleocapsid protein TP1, type I-C Cas4
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Metals Ions
Metals Ions on EC 3.1.12.1 - 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
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iron-sulfur centre
K+
nuclease activity of the enzyme is maximal in the presence of 20-200 mM KCl
Mg2+
Mn2+
additional information
iron-sulfur centre
near the active site, each enzyme protomer contains one [4Fe-4S] cluster, which is important for both maintaining the decameric state and nuclease activity
cleavage of a 15T DNA oligonucleotide by Sso0001 is observed in the presence of either magnesium or manganese, yielding a cluster of products of around 15 nt in size. A 20U RNA oligonucleotide is cleaved in the presence of manganese but not magnesium
Mg2+
nuclease activity of the enzyme is maximal in the presence of Mg2+ or Mn2+ (5 mM)
cleavage of a 15T DNA oligonucleotide by Sso0001 is observed in the presence of either magnesium or manganese, yielding a cluster of products of around 15 nt in size. A 20U RNA oligonucleotide is cleaved in the presence of manganese but not magnesium
Mn2+
nuclease activity of the enzyme is maximal in the presence of Mg2+ or Mn2+ (5 mM). Mn2+ is bound in the active site located inside the internal tunnel
Ca2+ does not support the nuclease activity
additional information
-
Ca2+ does not support the nuclease activity