Activating Compound | Comment | Organism | Structure |
---|---|---|---|
RecA protein | RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair | Escherichia coli | |
single-stranded DNA | RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair | Escherichia coli |
General Stability | Organism |
---|---|
At high protein concentrations, at low salt concentrations and at pH values of about 6-7, the protein forms a sticky precipitate that cannot be redissolved, to avoid this, the enzyme is maintained in 200 mM NaCl and the pH is kept at 7 or above | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
22700 | - |
E. coli | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Storage Stability | Organism |
---|---|
-70°C, stable | Escherichia coli |
5°C, 10 mM PIPES-NaOH, pH 7.0, 0.1 mM EDTA, 10% v/v glycerol, 200 mM NaCl, stable for long periods | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair | Escherichia coli | ? | - |
? | |
Repressor LexA + H2O | - |
Escherichia coli | LexA cleavage products | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
7 | - |
or above, stable | Escherichia coli |