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Literature summary for 3.1.11.1 extracted from

  • Lou, H.; Duan, Z.; Sun, T.; Huang, L.
    Cleavage of double-stranded DNA by the intrinsic 3-5 exonuclease activity of DNA polymerase B1 from the hyperthermophilic archaeon Sulfolobus solfataricus at high temperature (2004), FEMS Microbiol. Lett., 231, 111-117.
    View publication on PubMed
Search for more literature for 3.1.11.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Saccharolobus solfataricus

Inhibitors

Inhibitors Comment Organism Structure
NTP the strong 3'-5' exonuclease activity of polB1 is inhibited by 50% in the presence of 0.002 mM dNTPs, but remains measurable at up to 0.6 mM dNTPs Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P26811
-
-
Saccharolobus solfataricus P2 P26811
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dsDNA + H2O the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA Saccharolobus solfataricus ?
-
 ?
dsDNA + H2O the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA Saccharolobus solfataricus P2 ?
-
 ?
ssDNA + H2O the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA Saccharolobus solfataricus ?
-
 ?
ssDNA + H2O the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA Saccharolobus solfataricus P2 ?
-
 ?

Synonyms

Synonyms Comment Organism
Sso polB1
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Saccharolobus solfataricus

General Information

General Information Comment Organism
physiological function in view of the strong exonuclease activity of Sso polB1 on matched dsDNA, its is suggested that Sulfolobus solfataricus may have evolved mechanisms to regulate the exonuclease/polymerase ratio of the enzyme, thereby reducing the cost of proofreading at high temperature Saccharolobus solfataricus