Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Nakagawa, T.; Flores-Rozas, H.; Kolodner, R.D.
    The MER3 helicase involved in meiotic crossing over is stimulated by single-stranded DNA-binding proteins and unwinds DNA in the 3' to 5' direction. (2001), J. Biol. Chem., 276, 31487-31493.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.6.2.4 Double-stranded DNA MER3 ATPase activity is stimulated by either single- or double-stranded DNA Saccharomyces cerevisiae
5.6.2.4 single-stranded DNA MER3 ATPase activity is stimulated by either single- or double-stranded DNA Saccharomyces cerevisiae
5.6.2.4 single-stranded DNA-binding protein single-stranded DNA-binding proteins stimulate Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.6.2.4 single-stranded DNA-binding proteins
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.2.4 0.47
-
 ATP pH 7.6, 30°C, in presence of poly(dA) Saccharomyces cerevisiae
5.6.2.4 0.58
-
 ATP pH 7.6, 30°C, in presence of M13mp18 single-stranded circular DNA Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.4 Ca2+ MER3 ATPase activity requires a divalent cation. Maximal activity can be observed in the presence of either Ca2+, Mg2+, or Mn2+, whereas Zn2+ does not support the ATPase activity Saccharomyces cerevisiae
5.6.2.4 Mg2+ MER3 ATPase activity requires a divalent cation. Maximal activity can be observed in the presence of either Ca2+, Mg2+, or Mn2+, whereas Zn2+ does not support the ATPase activity Saccharomyces cerevisiae
5.6.2.4 Mn2+ MER3 ATPase activity requires a divalent cation. Maximal activity can be observed in the presence of either Ca2+, Mg2+, or Mn2+, whereas Zn2+ does not support the ATPase activity Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.2.4 ATP + H2O Saccharomyces cerevisiae meiosis-specific MER3 protein is required for crossing over, which ensures faithful segregation of homologous chromosomes at the first meiotic division ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.4 Saccharomyces cerevisiae P51979
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.2.4
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.4 ATP + H2O meiosis-specific MER3 protein is required for crossing over, which ensures faithful segregation of homologous chromosomes at the first meiotic division Saccharomyces cerevisiae ADP + phosphate
-
 ?
5.6.2.4 ATP + H2O unwinds DNA in the 3' to 5' direction relative to single-stranded regions in the DNA substrates Saccharomyces cerevisiae ADP + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.6.2.4 MER3 helicase
-
 Saccharomyces cerevisiae
5.6.2.4 MER3 protein
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.2.4 30
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6.2.4 8.8
-
 ATP pH 7.6, 30°C, in presence of M13mp18 single-stranded circular DNA Saccharomyces cerevisiae
5.6.2.4 9.2
-
 ATP pH 7.6, 30°C, in presence of poly(dA) Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6.2.4 7.6
-
 assay at Saccharomyces cerevisiae