EC Number |
Posttranslational Modification |
Reference |
---|
3.4.21.88 | more |
crosslinked with glutaraldehyde |
683784 |
3.4.21.88 | more |
LexA undergoes posttranslational modifications resulting in protein species with different pI values |
717734 |
3.4.21.88 | proteolytic modification |
protein undergoes self-cleavage reaction that requires RecA protein or occurs spontaneously at high pH-value. Cleavage site has two distinct and highly ordered conformations |
664539 |
3.4.21.88 | proteolytic modification |
RecA binds to and polymerizes on single-stranded DNA, which is a product of DNA damage. As a complex, it activates the autocleavage of LexA thereby lifting repression of SOS genes under DNA-damage conditions |
-, 755567 |
3.4.21.88 | proteolytic modification |
recombinant activated RecA-dependent LexA repressor self-cleavage |
-, 754924 |
3.4.21.88 | proteolytic modification |
repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88 |
-, 731931 |
3.4.21.88 | proteolytic modification |
the autocatalytic cleavage of MtLexA and the mutant proteins is analyzed, effects of pH and temperature, the enzyme is autocatalytically active at pH 9.5-11.0 and at up to 55°C |
-, 752390 |