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Literature summary for 5.6.2.4 extracted from

  • Toseland, C.P.; Martinez-Senac, M.M.; Slatter, A.F.; Webb, M.R.
    The ATPase cycle of PcrA helicase and its coupling to translocation on DNA (2009), J. Mol. Biol., 392, 1020-1032.
    View publication on PubMed
Search for more literature for 5.6.2.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information KM-values for cleavage of dTn DNA (dT10, dT20, dT30, dT40) Geobacillus stearothermophilus
0.0026
-
 2'(3')-O-(N-methylanthraniloyl)ATP pH 7.5, 20°C, in presence of DNA Geobacillus stearothermophilus
0.0035
-
 ATP pH 7.5, 20°C, in presence of DNA Geobacillus stearothermophilus
0.005
-
 ATP pH 7.5, 20°C, without DNA Geobacillus stearothermophilus
0.006
-
 2'(3')-O-(N-methylanthraniloyl)ATP pH 7.5, 20°C, without DNA Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Geobacillus stearothermophilus
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P56255
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'(3')-O-(N-methylanthraniloyl)ATP + H2O the fluorescent ATP analogue is used throughout all experiments to provide a complete ATPase cycle for a single nucleotide species Geobacillus stearothermophilus 2'(3')-O-(N-methylanthraniloyl)ADP + phosphate
-
 ?
ATP + H2O
-
 Geobacillus stearothermophilus ADP + phosphate
-
 ?
ATP + H2O the chemical cleavage step is the rate-limiting step in the ATPase cycle and is essentially irreversible and results in the bound ATP complex being a major component at steady state. This cleavage step is greatly accelerated by bound DNA, producing the high activation of this protein compared to the protein alone. The data suggest the possibility that ADP is released in two steps, which results in bound ADP also being a major intermediate, with bound ADP*phosphate being a very small component. It therefore seems likely that the major transition in structure occurs during the cleavage step, rather than phosphate release Geobacillus stearothermophilus ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
helicase PcrA
-
 Geobacillus stearothermophilus
PcrA helicase
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover numbers for cleavage of dTn DNA (dT10, dT20, dT30, dT40) Geobacillus stearothermophilus
0.1
-
 2'(3')-O-(N-methylanthraniloyl)ATP pH 7.5, 20°C, without DNA Geobacillus stearothermophilus
0.3
-
 ATP pH 7.5, 20°C, without DNA Geobacillus stearothermophilus
16.9
-
 ATP pH 7.5, 20°C, in presence of DNA Geobacillus stearothermophilus
17.2
-
 2'(3')-O-(N-methylanthraniloyl)ATP pH 7.5, 20°C, in presence of DNA Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Geobacillus stearothermophilus