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Literature summary for 5.6.2.4 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
Search for more literature for 5.6.2.4

Activating Compound

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

Inhibitors

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P51979
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
ATP + H2O unwinds DNA in the 3' to 5' direction relative to single-stranded regions in the DNA substrates Saccharomyces cerevisiae ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
MER3 helicase
-
 Saccharomyces cerevisiae
MER3 protein
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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