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Literature summary for 3.4.21.B30 extracted from

  • Mustard, J.A.; Little, J.W.
    Analysis of Escherichia coli RecA interactions with LexA, lambda CI, and UmuD by site-directed mutagenesis of recA (2000), J. Bacteriol., 182, 1659-1670.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli binds to a cleft located between two RecA monomers in the crystal structure ?
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD', K232A/E235A mutant of RecA cleaves UmuD more efficiently than wild-type RecA, T242A/R234A mutant of RecA is defective for cleavage of UmuD Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information binds to a cleft located between two RecA monomers in the crystal structure Escherichia coli ?
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?