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Literature summary for 5.6.2.3 extracted from

  • Jongeneel, C.; Formosa, T.; Alberts, B.
    Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein (1984), J. Biol. Chem., 259, 12925-12932 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DNA single-stranded DNA stimulates the enzyme 5-10times better than double-stranded DNA Tequatrovirus T4

Inhibitors

Inhibitors Comment Organism Structure
adenosine 5 O-(3-thiotriphosphate) inhibits ATP hydrolysis activity by more than 98% Tequatrovirus T4
KCl the enzyme is inhibited by salt concentrations in excess of 100 mM Tequatrovirus T4
additional information not inhibited by adenyl-5-yl (beta,gamma-methy1ene)diphosphonate Tequatrovirus T4
T4 gene 32 protein the T4 gene 32 protein, a single-strand-binding, helix-destabilizing protein, competes with the enzyme for binding to single-stranded DNA. Consequently, it seems to inhibit rather than to promote the helicase reaction Tequatrovirus T4

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the requirement for Mg2+ is absolute and maximal reaction rates are obtained when the Mg2+ concentration equals the ATP concentration Tequatrovirus T4

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE cellulose column chromatography, hydroxyapatite column chromatography, single-stranded DNA-cellulose column chromatography, Norleucine-Sepharose column chromatography, and Mono Q column chromatography Tequatrovirus T4

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.2
-
crude extract, at pH 7.5 and 37°C Tequatrovirus T4
162
-
after 810fold purification, at pH 7.5 and 37°C Tequatrovirus T4

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA the enzyme is a DNA-dependent ATPase and a DNA helicase. DNA in a single-stranded form is strongly preferred. The enzyme can unwind extensive stretches of double-stranded DNA very rapidly, appearing to move with a 5'-3' polarity relative to the single DNA strand to which it initially binds. The protein hydrolyzes ATP and dATP to their respective nucleoside diphosphates in the presence of DNA. Other nucleotides are not detectably hydrolyzed Tequatrovirus T4 ?
-
?

Synonyms

Synonyms Comment Organism
dda protein
-
Tequatrovirus T4

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 the enzyme is active over a broad pH range, remaining relatively unaffected between pH 6.0 and 9.0 Tequatrovirus T4

Cofactor

Cofactor Comment Organism Structure
ATP the enzyme reaction is entirely dependent on the presence of ATP or dATP Tequatrovirus T4
dATP the enzyme reaction is entirely dependent on the presence of ATP or dATP Tequatrovirus T4

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
200
-
at pH pH 7.5 and 37°C Tequatrovirus T4 KCl