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BRENDA support

Literature summary for 3.4.21.B30 extracted from

  • Foti, J.J.; Delucia, A.M.; Joyce, C.M.; Walker, G.C.
    UmuD2 inhibits a non-covalent step during DinB-mediated template slippage on homopolymeric nucleotide runs (2010), J. Biol. Chem., 285, 23086-23095.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Synonyms

Synonyms Comment Organism
UmuD2
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Escherichia coli

General Information

General Information Comment Organism
physiological function UmuD2, when bound to DinB, displaces the equilibrium in favor of the non-slipped conformation, thereby preventing frameshifting and potentially enhancing DinB activity on non-slipped substrates. DinB template slippage is inhibited by UmuD2 Escherichia coli