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Literature summary for 5.6.2.4 extracted from

  • Guo, X.; Huang, L.
    A superfamily 3 DNA helicase encoded by plasmid pSSVi from the hyperthermophilic archaeon Sulfolobus solfataricus unwinds DNA as a higher-order oligomer and interacts with host primase (2010), J. Bacteriol., 192, 1853-1864.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
E307A inactive in DNA unwinding and partially active in the ATPase assay Saccharolobus solfataricus
K265A/E307A completely abolished ATPase activity Saccharolobus solfataricus
K265A/R372I completely abolished ATPase activity Saccharolobus solfataricus
R372I very low levels of ATPase activity and no helicase activity Saccharolobus solfataricus

Inhibitors

Inhibitors Comment Organism Structure
NaCl above 100 mM Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme requires a divalent cation (Mg2+, Mn2+, or Ca2+) for its helicase activity, with Mg2+ being the preferred cofactor. The enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP) Saccharolobus solfataricus

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA Saccharolobus solfataricus ADP + phosphate
-
?
ATP + H2O the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA Saccharolobus solfataricus P2 ADP + phosphate
-
?

Subunits

Subunits Comment Organism
oligomer the enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP). Both N-terminal and C-terminal portions of ORF735 (87 and 160 amino acid residues, respectively, in size) are required for protein dimerization but dispensable for the formation of the higher-order oligomer. The protein unwinds DNA only as a large oligomer Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
ORF735 protein
-
Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharolobus solfataricus