Literature summary for 3.1.11.1 extracted from

Lou, H.; Duan, Z.; Huo, X.; Huang, L.
Modulation of hyperthermophilic DNA polymerase activity by archaeal chromatin proteins (2003), J. Biol. Chem., 279, 127-132.

Search for more literature for 3.1.11.1

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	7-kDa DNA-binding proteins are capable of significantly inhibiting the excision and enhancing the extension of matched template primers by the polymerase. The proteins do not protect single-stranded DNA from cleavage by polB1. The 7-kDa proteins do not affect the proofreading ability of polB1 and are not inhibitory to the excision of mismatched primers by the polymerase. The dNTP concentrations required for the effective inhibition of the 3'-5' exonuclease activity of polB1 are lowered from 1 mM in the absence of the 7-kDa proteins to 50 M in the presence of the proteins at 65 °C	Saccharolobus solfataricus

Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
single-stranded DNA + H2O	3'-5' exonuclease activity, degrades both single-stranded DNA and double-stranded DNA at similar rates	Saccharolobus solfataricus	?	-	?
single-stranded DNA + H2O	3'-5' exonuclease activity, degrades both single-stranded DNA and double-stranded DNA at similar rates	Saccharolobus solfataricus P2	?	-	?

Synonyms

Synonyms	Comment	Organism
POlB1	-	Saccharolobus solfataricus
SSO0552	locus name	Saccharolobus solfataricus

Temperature Optimum [°C]

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

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Release 2023.1 (January 2023)