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Literature summary for 3.4.21.88 extracted from

  • Little, J.W.; Kim, B.; Roland, K.L.; Smith, M.H.; Lin, L.L.; Slilaty, S.N.
    Cleavage of LexA repressor (1994), Methods Enzymol., 244, 266-284.
    View publication on PubMed
Search for more literature for 3.4.21.88

Activating Compound

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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
22700
-
 E. coli Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Storage Stability

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 and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
7
-
 or above, stable Escherichia coli